ArchDB - Biological DataBase of Protein Loops

Information on SUBCLASS 1.1.3

Subclass Accession number: 21
Subclass: 1.1.3
Type: EH beta-alpha
DB: ArchDB-KI

Number of loops: 7

Average sequence ID (%) : 26.2 +/- 9.1
Average RMSD (Å) : 0.36 +/- 0.21

Consensus geometry

d (Å): 5

delta (°): 0-45

theta (°): 45-90

rho (°): 225-270

Consensus Sequence:	hhXhp
(φψ)-conformation:	bppaa

Pattern:	x	{AI}	[GILV]	x	{FGP}	{DEN}	[AGM]	{CILV}
Conservation:	-1.078	1.617	0.575	-0.298	-1.447	0.130	0.783	-0.281

Loops included in this Subclass

Loop	PDB	Chain	Start	End	Sequence	Sec Struct	Ramachandran
1b7b_A_4	1b7b	A	7	14	VALGGNAI	EEE-HHHH	bbxxaaaa
1be4_A_6	1be4	A	9	16	IAIKPDGV	EEE-HHHH	bbxxaaaa
1ehw_B_6	1ehw	B	9	16	VAVKPDGV	EEE-HHHH	bbxxaaaa
1hdi_A_183	1hdi	A	183	190	KAGAFLMK	EEE-HHHH	bbxxaaaa
1kbl_A_39	1kbl	A	40	47	FTVTTEAC	EEE-HHHH	bbxxaaaa
1nhk_R_3	1nhk	R	8	15	SIIKPDGL	EEE-HHHH	bbxxaaaa
1nue_A_6	1nue	A	9	16	IAIKPDGV	EEE-HHHH	bbxxaaaa

PDB ligands within a cut-off distance of 6 Å in this subclass

Loop	PDB	Chain	Ligands	Residue
1be4_A_6	1be4	A	PCGCYCLIC GUANOSINE MONOPHOSPHATE	K - 12
1nhk_R_3	1nhk	R	CMPADENOSINE-3',5'-CYCLIC-MONOPHOSPHATE	K - 11
1nue_A_6	1nue	A	GDPGUANOSINE-5'-DIPHOSPHATE	K - 12

PDB Site Annotated loops in this subclass

Loop	PDB	Chain	Site	Residue
1be4_A_6	1be4	A	NULC-GMP BINDING SITE.	K - 12

Bibliographic annotations

Loop	PDB	Chain	Annotation	Residue
1b7b_A_4	1b7b RefA.MARINA,P.M.ALZARI,J.BRAVO,M.URIARTE,B.BARCELONA,I.FITA,V.RUBIO. CARBAMATE KINASE: NEW STRUCTURAL MACHINERY FOR MAKING CARBAMOYL PHOSPHATE, THE COMMON PRECURSOR OF PYRIMIDINES AND ARGININE PROTEIN SCI. v.8;934,1999	A	CONSERVED RESIDUE	L - 9
1b7b_A_4	1b7b RefA.MARINA,P.M.ALZARI,J.BRAVO,M.URIARTE,B.BARCELONA,I.FITA,V.RUBIO. CARBAMATE KINASE: NEW STRUCTURAL MACHINERY FOR MAKING CARBAMOYL PHOSPHATE, THE COMMON PRECURSOR OF PYRIMIDINES AND ARGININE PROTEIN SCI. v.8;934,1999	A	CONSERVED RESIDUE	G - 10
1b7b_A_4	1b7b RefA.MARINA,P.M.ALZARI,J.BRAVO,M.URIARTE,B.BARCELONA,I.FITA,V.RUBIO. CARBAMATE KINASE: NEW STRUCTURAL MACHINERY FOR MAKING CARBAMOYL PHOSPHATE, THE COMMON PRECURSOR OF PYRIMIDINES AND ARGININE PROTEIN SCI. v.8;934,1999	A	PUTATIVE ACTIVE SITE RESIDUE	G - 11
1b7b_A_4	1b7b RefA.MARINA,P.M.ALZARI,J.BRAVO,M.URIARTE,B.BARCELONA,I.FITA,V.RUBIO. CARBAMATE KINASE: NEW STRUCTURAL MACHINERY FOR MAKING CARBAMOYL PHOSPHATE, THE COMMON PRECURSOR OF PYRIMIDINES AND ARGININE PROTEIN SCI. v.8;934,1999	A	CONSERVED RESIDUE	A - 13
1b7b_A_4	1b7b RefA.MARINA,P.M.ALZARI,J.BRAVO,M.URIARTE,B.BARCELONA,I.FITA,V.RUBIO. CARBAMATE KINASE: NEW STRUCTURAL MACHINERY FOR MAKING CARBAMOYL PHOSPHATE, THE COMMON PRECURSOR OF PYRIMIDINES AND ARGININE PROTEIN SCI. v.8;934,1999	A	CONSERVED RESIDUE	A - 13
1b7b_A_4	1b7b RefA.MARINA,P.M.ALZARI,J.BRAVO,M.URIARTE,B.BARCELONA,I.FITA,V.RUBIO. CARBAMATE KINASE: NEW STRUCTURAL MACHINERY FOR MAKING CARBAMOYL PHOSPHATE, THE COMMON PRECURSOR OF PYRIMIDINES AND ARGININE PROTEIN SCI. v.8;934,1999	A	CONSERVED RESIDUE	I - 14
1nhk_R_3	1nhk RefR.L.WILLIAMS,D.A.OREN,J.MUNOZ-DORADO,S.INOUYE,E.ARNOLD. CRYSTAL STRUCTURE OF MYXOCOCCUS XANTHUS NUCLEOSIDE DIPHOSPHATE KINASE AND ITS INTERACTION WITH A NUCLEOTIDE SUSTRATE AT 2.0 A RESOLUTION J.MOL.BIOL. v.234;1230,1993	R	ATP BINDING RESIDUE	K - 11

Clusters included in this Subclass

CLUSTER: EH.0.4