Logo
Information on SUBCLASS 0.1.1
Subclass Accession number: 13
Subclass: 0.1.1
Type: EH beta-alpha
DB: ArchDB-KI
 Number of loops: 18

Average sequence ID (%) : 36.7 +/- 8.2
Average RMSD (Å) : 0.32 +/- 0.16

Consensus geometry
d (Å): 3 delta (°): 0-45 theta (°): 45-90 rho (°): 135-180
Consensus Sequence: hpXG
(φψ)-conformation: bbaa
Pattern: {FILV}{DNS}x{DG}{DKQR}[AFILMY]{FLMY}{DQR}x
Conservation:-0.6361.297-0.5561.712-1.0900.384-0.5670.389-0.932
Loops included in this Subclass
LoopPDBChainStartEndSequenceSec StructRamachandran
1ak2_*_431ak2   -4553LATGDMLRAEEHHHHHHHbbaaaaaaa
1ake_A_281ake   A2937ISTGDMLRAEEHHHHHHHbbaaaaaaa
1aky_*_311aky   -3341LATGDMLRSEEHHHHHHHbbaaaaaaa
1bo1_A_2811bo1   A286294HDVDRAEQEEEHHHHHHHbxaaaaaaa
1cke_A_321cke   A3442LDSGAIYRVEEHHHHHHHbbaaaaaaa
1dvr_A_311dvr   A3341LATGDMLRSEEHHHHHHHbbaaaaaaa
1hcl_*_851hcl   -8593QDLKKFMDAEEHHHHHHHbbaaaaaaa
1nks_A_321nks   A3543INYGDFMLAEEHHHHHHHbxaaaaaaa
1qf9_A_331qf9   A3543LSAGDLLRQEEHHHHHHHbxaaaaaaa
1shk_A_291shk   A3139VDTDIFMQHEEHHHHHHHbbaaaaaaa
1uke_*_331uke   -3543LSAGDLLRQEEHHHHHHHbxaaaaaaa
1uky_*_431uky   -4553LSAGDLLRAEEHHHHHHHbbaaaaaaa
1ukz_*_431ukz   -4553LSAGDLLRAEEHHHHHHHbbaaaaaaa
1zip_*_281zip   -2937ISTGDMFRAEEHHHHHHHbbaaaaaaa
2ak3_A_322ak3   A3442LSSGDLLRDEEHHHHHHHbbaaaaaaa
2cmk_A_322cmk   A3442LDSGAIYRVEEHHHHHHHbbaaaaaaa
3adk_*_353adk   -3745LSTGDLLRAEEHHHHHHHbbaaaaaaa
3bif_A_693bif   A7280FNVGQYRRDEEHHHHHHHbxaaaaaaa
PDB ligands within a cut-off distance of 6 Å in this subclass
LoopPDBChainLigandsResidue
1ake_A_281ake   A     AP5BIS(ADENOSINE)-5'-PENTAPHOSPHATE S - 30
1ake_A_281ake   A     AP5BIS(ADENOSINE)-5'-PENTAPHOSPHATE T - 31
1ake_A_281ake   A     AP5BIS(ADENOSINE)-5'-PENTAPHOSPHATE G - 32
1ake_A_281ake   A     AP5BIS(ADENOSINE)-5'-PENTAPHOSPHATE D - 33
1ake_A_281ake   A     AP5BIS(ADENOSINE)-5'-PENTAPHOSPHATE L - 35
1ake_A_281ake   A     AP5BIS(ADENOSINE)-5'-PENTAPHOSPHATE R - 36
1aky_*_311aky   *     IMDIMIDAZOLE H - 32
1aky_*_311aky   *     IMDIMIDAZOLE A - 34
1aky_*_311aky   *     AP5BIS(ADENOSINE)-5'-PENTAPHOSPHATE T - 35
1aky_*_311aky   *     AP5BIS(ADENOSINE)-5'-PENTAPHOSPHATE G - 36
1aky_*_311aky   *     IMDIMIDAZOLE G - 36
1aky_*_311aky   *     AP5BIS(ADENOSINE)-5'-PENTAPHOSPHATE D - 37
1aky_*_311aky   *     IMDIMIDAZOLE D - 37
1aky_*_311aky   *     AP5BIS(ADENOSINE)-5'-PENTAPHOSPHATE L - 39
1aky_*_311aky   *     AP5BIS(ADENOSINE)-5'-PENTAPHOSPHATE R - 40
1aky_*_311aky   *     IMDIMIDAZOLE R - 40
1qf9_A_331qf9   A     ALFTETRAFLUOROALUMINATE ION S - 36
1qf9_A_331qf9   A     MGMAGNESIUM ION S - 36
1qf9_A_331qf9   A     C5PCYTIDINE-5'-MONOPHOSPHATE S - 36
1qf9_A_331qf9   A     C5PCYTIDINE-5'-MONOPHOSPHATE A - 37
1qf9_A_331qf9   A     C5PCYTIDINE-5'-MONOPHOSPHATE G - 38
1qf9_A_331qf9   A     MGMAGNESIUM ION D - 39
1qf9_A_331qf9   A     C5PCYTIDINE-5'-MONOPHOSPHATE D - 39
1qf9_A_331qf9   A     C5PCYTIDINE-5'-MONOPHOSPHATE L - 41
1qf9_A_331qf9   A     ALFTETRAFLUOROALUMINATE ION R - 42
1qf9_A_331qf9   A     MGMAGNESIUM ION R - 42
1qf9_A_331qf9   A     C5PCYTIDINE-5'-MONOPHOSPHATE R - 42
1uke_*_331uke   *     MGMAGNESIUM ION H - 34
1uke_*_331uke   *     UP5P1-(ADENOSINE-5'-P5-(URIDINE-5')PENTAPHOSPHATE S - 36
1uke_*_331uke   *     MGMAGNESIUM ION S - 36
1uke_*_331uke   *     UP5P1-(ADENOSINE-5'-P5-(URIDINE-5')PENTAPHOSPHATE A - 37
1uke_*_331uke   *     UP5P1-(ADENOSINE-5'-P5-(URIDINE-5')PENTAPHOSPHATE G - 38
1uke_*_331uke   *     UP5P1-(ADENOSINE-5'-P5-(URIDINE-5')PENTAPHOSPHATE D - 39
1uke_*_331uke   *     MGMAGNESIUM ION D - 39
1uke_*_331uke   *     UP5P1-(ADENOSINE-5'-P5-(URIDINE-5')PENTAPHOSPHATE L - 41
1uke_*_331uke   *     UP5P1-(ADENOSINE-5'-P5-(URIDINE-5')PENTAPHOSPHATE R - 42
1uke_*_331uke   *     MGMAGNESIUM ION R - 42
1uky_*_431uky   *     ADPADENOSINE-5'-DIPHOSPHATE S - 46
1uky_*_431uky   *     ADPADENOSINE-5'-DIPHOSPHATE A - 47
1uky_*_431uky   *     ADPADENOSINE-5'-DIPHOSPHATE G - 48
1uky_*_431uky   *     ADPADENOSINE-5'-DIPHOSPHATE D - 49
1uky_*_431uky   *     ADPADENOSINE-5'-DIPHOSPHATE L - 51
1uky_*_431uky   *     ADPADENOSINE-5'-DIPHOSPHATE R - 52
1ukz_*_431ukz   *     AMPADENOSINE MONOPHOSPHATE S - 46
1ukz_*_431ukz   *     AMPADENOSINE MONOPHOSPHATE A - 47
1ukz_*_431ukz   *     AMPADENOSINE MONOPHOSPHATE G - 48
1ukz_*_431ukz   *     AMPADENOSINE MONOPHOSPHATE D - 49
1ukz_*_431ukz   *     AMPADENOSINE MONOPHOSPHATE L - 51
1ukz_*_431ukz   *     AMPADENOSINE MONOPHOSPHATE R - 52
1zip_*_281zip   *     AP5BIS(ADENOSINE)-5'-PENTAPHOSPHATE S - 30
1zip_*_281zip   *     MNMANGANESE (II) ION S - 30
1zip_*_281zip   *     AP5BIS(ADENOSINE)-5'-PENTAPHOSPHATE T - 31
1zip_*_281zip   *     AP5BIS(ADENOSINE)-5'-PENTAPHOSPHATE G - 32
1zip_*_281zip   *     AP5BIS(ADENOSINE)-5'-PENTAPHOSPHATE D - 33
1zip_*_281zip   *     MNMANGANESE (II) ION D - 33
1zip_*_281zip   *     AP5BIS(ADENOSINE)-5'-PENTAPHOSPHATE F - 35
1zip_*_281zip   *     AP5BIS(ADENOSINE)-5'-PENTAPHOSPHATE R - 36
1zip_*_281zip   *     MNMANGANESE (II) ION R - 36
2ak3_A_322ak3   A     AMPADENOSINE MONOPHOSPHATE S - 35
2ak3_A_322ak3   A     AMPADENOSINE MONOPHOSPHATE S - 36
2ak3_A_322ak3   A     AMPADENOSINE MONOPHOSPHATE G - 37
2ak3_A_322ak3   A     AMPADENOSINE MONOPHOSPHATE D - 38
2ak3_A_322ak3   A     AMPADENOSINE MONOPHOSPHATE L - 40
2ak3_A_322ak3   A     AMPADENOSINE MONOPHOSPHATE R - 41
PDB Site Annotated loops in this subclass
LoopPDBChainSiteResidue
1shk_A_291shk   A SASTHE ELECTRON DENSITY FOR SHIKIMATE WAS AMBIGUOUS PREVENTING ITS INCLUSION IN THE MODEL. THE LISTED RESIDUES ARE GROUPED AROUND THE DENSITY AND ARE MOST LIKELY TO BE PART OF THE SHIKIMATE BINDING.D - 34
Bibliographic annotations
LoopPDBChainAnnotationResidue
1ake_A_281ake   RefC.W.MUELLER,G.E.SCHULZ. STRUCTURE OF THE COMPLEX BETWEEN ADENYLATE KINASE FROM ESCHERICHIA COLI AND THE INHIBITOR AP=5=A REFINED AT 1.9 ANGSTROMS RESOLUTION: A MODEL FOR A CATALYTIC TRANSITION STATE  J.MOL.BIOL. v.224;159,1992AAMP BINDING RESIDUE R - 36
1cke_A_321cke   RefP.BRIOZZO,B.GOLINELLI-PIMPANEAU,A.M.GILLES,J.F.GAUCHER,S.BURLACU-MIRON,H.SAKAMOTO,J.JANIN,O.BARZU. STRUCTURES OF ESHERICHIA COLI CMP KINASE ALONE AND IN COMPLEX WITH CDP: A NEW FOLD OF THE NUCLEOSIDE MONOPHOSPHATE BINDING DOMAIN AND INSIGHTS INTO CYTOSINE NUCLEOSIDE SPECIFICITY  STRUCTURE (LONDON) v.6;1517,1998ACMP BINDING RESIDUE (SPECIFICITY)S - 36
1cke_A_321cke   RefP.BRIOZZO,B.GOLINELLI-PIMPANEAU,A.M.GILLES,J.F.GAUCHER,S.BURLACU-MIRON,H.SAKAMOTO,J.JANIN,O.BARZU. STRUCTURES OF ESHERICHIA COLI CMP KINASE ALONE AND IN COMPLEX WITH CDP: A NEW FOLD OF THE NUCLEOSIDE MONOPHOSPHATE BINDING DOMAIN AND INSIGHTS INTO CYTOSINE NUCLEOSIDE SPECIFICITY  STRUCTURE (LONDON) v.6;1517,1998APHOSPHATE BINDING RESIDUER - 41
1nks_A_321nks   RefC.VONRHEIN,H.BOENISCH,G.SCHAEFER,G.E.SCHULZ. THE STRUCTURE OF A TRIMERIC ARCHAEAL ADENYLATE KINASE  J.MOL.BIOL. v.282;167,1998AP-MNP BINDING RESIDUEN - 32
1nks_A_321nks   RefC.VONRHEIN,H.BOENISCH,G.SCHAEFER,G.E.SCHULZ. THE STRUCTURE OF A TRIMERIC ARCHAEAL ADENYLATE KINASE  J.MOL.BIOL. v.282;167,1998ANMP BASE BINDING RESIDUE M - 41
1shk_A_291shk   RefT.KRELL,J.E.COYLE,M.J.HORSBURGH,J.R.COGGINS,A.J.LAPTHORN. CRYSTALLIZATION AND PRELIMINARY X-RAY CRYSTALLOGRAPHIC ANALYSIS OF SHIKIMATE KINASE FROM ERWINIA CHRYSANTHEMI  ACTA CRYSTALLOGR.,SECT.D v.53;612,1997AMg ION BINDING RESIDUED - 32
1shk_A_291shk   RefT.KRELL,J.E.COYLE,M.J.HORSBURGH,J.R.COGGINS,A.J.LAPTHORN. CRYSTALLIZATION AND PRELIMINARY X-RAY CRYSTALLOGRAPHIC ANALYSIS OF SHIKIMATE KINASE FROM ERWINIA CHRYSANTHEMI  ACTA CRYSTALLOGR.,SECT.D v.53;612,1997AMg ION BINDING RESIDUED - 34
2cmk_A_322cmk   RefP.BRIOZZO,B.GOLINELLI-PIMPANEAU,J.F.GAUCHER,A.M.GILLES,S.BURLACU-MIRON,H.SAKAMOTO,J.JANIN,O.BARZU. STRUCTURES OF ESHERICHIA COLI CMP KINASE ALONE AND IN COMPLEX WITH CDP: A NEW FOLD OF THE NUCLEOSIDE MONOPHOSPHATE BINDING DOMAIN AND INSIGHTS INTO CYTOSINE NUCLEOTIDE SPECIFICITY  STRUCTURE (LONDON) v.6;1517,1998ACMP BINDING RESIDUE (SPECIFICITY)S - 36
2cmk_A_322cmk   RefP.BRIOZZO,B.GOLINELLI-PIMPANEAU,J.F.GAUCHER,A.M.GILLES,S.BURLACU-MIRON,H.SAKAMOTO,J.JANIN,O.BARZU. STRUCTURES OF ESHERICHIA COLI CMP KINASE ALONE AND IN COMPLEX WITH CDP: A NEW FOLD OF THE NUCLEOSIDE MONOPHOSPHATE BINDING DOMAIN AND INSIGHTS INTO CYTOSINE NUCLEOTIDE SPECIFICITY  STRUCTURE (LONDON) v.6;1517,1998APHOSPHATE BINDING RESIDUER - 41
3bif_A_693bif   RefM.H.YUEN,X.WANG,H.MIZUGUCHI,K.UYEDA,C.A.HASEMANN. A SWITCH IN THE KINASE DOMAIN OF RAT TESTIS 6-PHOSPHOFRUCTO-2-KINASE/FRUCTOSE- 2,6-BISPHOSPHATASE  BIOCHEMISTRY v.38;12333,1999AF6P BINDING RESIDUER - 78

Clusters included in this Subclass
CLUSTER: EH.0.0
CLUSTER: EH.0.7