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Information on SUBCLASS 4.5.1
Subclass Accession number: 173
Subclass: 4.5.1
Type: HH alpha-alpha
DB: ArchDB-KI
Number of loops: 5

Average sequence ID (%) : 15.8 +/- 1.8
Average RMSD (Å) : 1.55 +/- 0.79

Consensus geometry
d (Å): 9 delta (°): 90-135 theta (°): 90-135 rho (°): 315-360
Consensus Sequence: LhXXXPXX
(φψ)-conformation: aapgbpaa
Pattern: [FIL]{ERST}x[LV][CFLV]x{DG}{AFK}{P}xx[AEF][ACVY]x{RY}[AFLM]x{HKY}[ACMY]
Conservation:1.110-0.319-0.7521.8510.168-0.8310.883-0.5882.546-1.145-0.844-0.578-0.226-1.089-0.1350.139-0.4760.617-0.332
Loops included in this Subclass
LoopPDBChainStartEndSequenceSec StructRamachandran
1bx4_A_2951bx4   A307325LSQLVSDKPLTECIRAGHYHHHHTTT--HHHHHHHHHHaaaaaavbxaaaaaaaaaa
1cki_A_2421cki   A242260IEVLCKGYPSEFATYLNFCHHHHTTTS-HHHHHHHHHHaaaaapvbpaaaaaaaaaa
1rkd_*_2531rkd   -262280ITALLEEKPLPEAIRFAHAHHHHHTT--HHHHHHHHHHaaaaaavxxaaaaaaaaaa
1wfc_*_2701wfc   -270288FANVFIGANPLAVDLLEKMHHHHSTTS-HHHHHHHHHHaaaabpvxxaaaaaaaaaa
2csn_*_2422csn   -242260LRELCAGFPEEFYKYMHYAHHHHSTTS-HHHHHHHHHHaaaaapgb-aaaaaaaaaa
PDB ligands within a cut-off distance of 6 Å in this subclass
LoopPDBChainLigandsResidue
1bx4_A_2951bx4   A     MO6MAGNESIUM ION, 6 WATERS COORDINATED T - 295
1bx4_A_2951bx4   A     ADNADENOSINE T - 295
1bx4_A_2951bx4   A     MO6MAGNESIUM ION, 6 WATERS COORDINATED N - 296
1bx4_A_2951bx4   A     ADNADENOSINE N - 296
1bx4_A_2951bx4   A     MO6MAGNESIUM ION, 6 WATERS COORDINATED G - 297
1bx4_A_2951bx4   A     ADNADENOSINE G - 297
1bx4_A_2951bx4   A     MO6MAGNESIUM ION, 6 WATERS COORDINATED A - 298
1bx4_A_2951bx4   A     ADNADENOSINE A - 298
1bx4_A_2951bx4   A     MO6MAGNESIUM ION, 6 WATERS COORDINATED G - 299
1bx4_A_2951bx4   A     ADNADENOSINE G - 299
1bx4_A_2951bx4   A     MO6MAGNESIUM ION, 6 WATERS COORDINATED D - 300
1bx4_A_2951bx4   A     ADNADENOSINE D - 300
1bx4_A_2951bx4   A     ADNADENOSINE F - 302
1bx4_A_2951bx4   A     MO6MAGNESIUM ION, 6 WATERS COORDINATED V - 303
1bx4_A_2951bx4   A     ADNADENOSINE G - 323
1bx4_A_2951bx4   A     ADNADENOSINE H - 324
1bx4_A_2951bx4   A     ADNADENOSINE A - 327
1bx4_A_2951bx4   A     ADNADENOSINE S - 328
1rkd_*_2531rkd   *     ADPADENOSINE-5'-DIPHOSPHATE A - 253
1rkd_*_2531rkd   *     ADPADENOSINE-5'-DIPHOSPHATE G - 254
1rkd_*_2531rkd   *     ADPADENOSINE-5'-DIPHOSPHATE D - 255
1rkd_*_2531rkd   *     RIBRIBOSE D - 255
1rkd_*_2531rkd   *     ADPADENOSINE-5'-DIPHOSPHATE F - 257
1rkd_*_2531rkd   *     ADPADENOSINE-5'-DIPHOSPHATE N - 258
1rkd_*_2531rkd   *     ADPADENOSINE-5'-DIPHOSPHATE A - 278
1rkd_*_2531rkd   *     ADPADENOSINE-5'-DIPHOSPHATE H - 279
1rkd_*_2531rkd   *     ADPADENOSINE-5'-DIPHOSPHATE A - 280
1rkd_*_2531rkd   *     ADPADENOSINE-5'-DIPHOSPHATE A - 282
1rkd_*_2531rkd   *     ADPADENOSINE-5'-DIPHOSPHATE A - 283
1rkd_*_2531rkd   *     ADPADENOSINE-5'-DIPHOSPHATE V - 286
PDB Site Annotated loops in this subclass
LoopPDBChainSiteResidue
1rkd_*_2531rkd   * AB3RESIDUES WITHIN VAN DER WAALS DISTANCE OF ADP.A - 253
1rkd_*_2531rkd   * RB2RESIDUES MAKING WATER-MEDIATED HYDROGEN BONDS WITH RIBOSE.G - 254
1rkd_*_2531rkd   * RB1RESIDUES MAKING DIRECT HYDROGEN BONDS WITH RIBOSE.D - 255
1rkd_*_2531rkd   * RB2RESIDUES MAKING WATER-MEDIATED HYDROGEN BONDS WITH RIBOSE.D - 255
1rkd_*_2531rkd   * AB1RESIDUES MAKING DIRECT HYDROGEN BONDS WITH ADP.A - 280
1rkd_*_2531rkd   * AB2RESIDUES MAKING WATER-MEDIATED HYDROGEN BONDS WITH ADP.A - 280
1rkd_*_2531rkd   * AB3RESIDUES WITHIN VAN DER WAALS DISTANCE OF ADP.A - 282
1rkd_*_2531rkd   * AB3RESIDUES WITHIN VAN DER WAALS DISTANCE OF ADP.V - 286
Bibliographic annotations
LoopPDBChainAnnotationResidue
1bx4_A_2951bx4   RefI.I.MATHEWS,M.D.ERION,S.E.EALICK. STRUCTURE OF HUMAN ADENOSINE KINASE AT 1.5 A RESOLUTION  BIOCHEMISTRY v.37;15607,1998AATP BINDING RESIDUET - 295
1bx4_A_2951bx4   RefI.I.MATHEWS,M.D.ERION,S.E.EALICK. STRUCTURE OF HUMAN ADENOSINE KINASE AT 1.5 A RESOLUTION  BIOCHEMISTRY v.37;15607,1998AMg ION BINDING RESIDUET - 295
1bx4_A_2951bx4   RefI.I.MATHEWS,M.D.ERION,S.E.EALICK. STRUCTURE OF HUMAN ADENOSINE KINASE AT 1.5 A RESOLUTION  BIOCHEMISTRY v.37;15607,1998AMg ION BINDING RESIDUEN - 296
1bx4_A_2951bx4   RefI.I.MATHEWS,M.D.ERION,S.E.EALICK. STRUCTURE OF HUMAN ADENOSINE KINASE AT 1.5 A RESOLUTION  BIOCHEMISTRY v.37;15607,1998ACATALYTIC RESIDUED - 300
1bx4_A_2951bx4   RefI.I.MATHEWS,M.D.ERION,S.E.EALICK. STRUCTURE OF HUMAN ADENOSINE KINASE AT 1.5 A RESOLUTION  BIOCHEMISTRY v.37;15607,1998AATP BINDING RESIDUEF - 302
1bx4_A_2951bx4   RefI.I.MATHEWS,M.D.ERION,S.E.EALICK. STRUCTURE OF HUMAN ADENOSINE KINASE AT 1.5 A RESOLUTION  BIOCHEMISTRY v.37;15607,1998AATP BINDING RESIDUEH - 324
1bx4_A_2951bx4   RefI.I.MATHEWS,M.D.ERION,S.E.EALICK. STRUCTURE OF HUMAN ADENOSINE KINASE AT 1.5 A RESOLUTION  BIOCHEMISTRY v.37;15607,1998AATP BINDING RESIDUEA - 327
1bx4_A_2951bx4   RefI.I.MATHEWS,M.D.ERION,S.E.EALICK. STRUCTURE OF HUMAN ADENOSINE KINASE AT 1.5 A RESOLUTION  BIOCHEMISTRY v.37;15607,1998AATP BINDING RESIDUEA - 327

Clusters included in this Subclass
CLUSTER: HH.4.2
CLUSTER: HH.4.8