ArchDB - Biological DataBase of Protein Loops

Information on SUBCLASS 3.2.1

Subclass Accession number: 121
Subclass: 3.2.1
Type: HE alpha-beta
DB: ArchDB-KI

Number of loops: 8

Average sequence ID (%) : 11.8 +/- 0.6
Average RMSD (Å) : 0.86 +/- 0.39

Consensus geometry

d (Å): 9

delta (°): 90-135

theta (°): 135-180

rho (°): 45-90

Consensus Sequence:	pXGXpXh
(φψ)-conformation:	aagpabb

Pattern:	x	{GILM}	x	{AILV}	x	x	{ACFGL}	x	{EKL}	x	{GN}	x	{DEKN}	x	{AIV}	{AFIMWY}	[ACFIL]
Conservation:	-0.554	-0.658	-0.386	0.520	-0.620	-0.605	-0.405	-0.396	1.134	-0.987	3.096	-0.414	0.824	-0.666	0.296	-0.602	0.426

Loops included in this Subclass

Loop	PDB	Chain	Start	End	Sequence	Sec Struct	Ramachandran
1dku_A_230	1dku	A	233	249	TLAANALVENGAKEVYA	HHHHHHHHHTT-SEEEE	aaaaaaaaaagxabbbb
1dku_A_68	1dku	A	76	92	LIMVDALKRASAKTINI	HHHHHHHHHTT-SEEEE	aaaaaaaaaavpabbbx
1e0t_A_172	1e0t	A	175	191	KQDLIFGCEQGVDFVAA	HHHHHHHHHHT-SEEEE	aaaaaaaaaavxabbxx
1e0t_A_292	1e0t	A	295	311	AGDVANAILDGTDAVML	HHHHHHHHHHT-SEEEE	aaaaaaaaaagpabbxb
1e19_A_274	1e19	A	278	294	VLAAIRFIEWGGERAII	HHHHHHHHHHT-SEEEE	aaaaaaaaaagxabbbb
1gc5_A_78	1gc5	A	82	98	LGGILRSIKLGKAMEWF	HHHHHHHHHS---EEEE	aaaaaaaaaalbxbbbx
1i58_B_365	1i58	B	367	383	RMVRDLAKKMNKEVNFI	HHHHHHHHHTT--EEEE	aaaaaaaaaalbbbbxb
1kbl_A_838	1kbl	A	838	854	PSSVEFCHKVGLNYVSC	HHHHHHHHHTT-SEEEE	aaaaaaaaaavxabbbb

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

Loop	PDB	Chain	Ligands	Residue
1e19_A_274	1e19	A	ADPADENOSINE-5'-DIPHOSPHATE	M - 274
1e19_A_274	1e19	A	ADPADENOSINE-5'-DIPHOSPHATE	G - 275
1e19_A_274	1e19	A	ADPADENOSINE-5'-DIPHOSPHATE	K - 277
1e19_A_274	1e19	A	MGMAGNESIUM ION	K - 277

Bibliographic annotations

Loop	PDB	Chain	Annotation	Residue
1dku_A_68	1dku RefT.A.ERIKSEN,A.KADZIOLA,A.-K.BENTSEN,K.W.HARLOW,S.LARSEN. STRUCTURAL BASIS FOR THE FUNCTION OF BACILLUS SUBTILIS PHOSPHORIBOSYL-PYROPHOSPHATE SYNTHETASE NAT.STRUCT.BIOL. v.7;303,2000	A	REGULATORY ADP BINDING RESIDUE	A - 85
1dku_A_68	1dku RefT.A.ERIKSEN,A.KADZIOLA,A.-K.BENTSEN,K.W.HARLOW,S.LARSEN. STRUCTURAL BASIS FOR THE FUNCTION OF BACILLUS SUBTILIS PHOSPHORIBOSYL-PYROPHOSPHATE SYNTHETASE NAT.STRUCT.BIOL. v.7;303,2000	A	REGULATORY ADP BINDING RESIDUE	A - 85
1dku_A_68	1dku RefT.A.ERIKSEN,A.KADZIOLA,A.-K.BENTSEN,K.W.HARLOW,S.LARSEN. STRUCTURAL BASIS FOR THE FUNCTION OF BACILLUS SUBTILIS PHOSPHORIBOSYL-PYROPHOSPHATE SYNTHETASE NAT.STRUCT.BIOL. v.7;303,2000	A	REGULATORY ADP BINDING RESIDUE	S - 86
1e19_A_274	1e19 RefS.RAMON-MAIQUES,A.MARINA,M.URIARTE,I.FITA,V.RUBIO. THE 1.5-A RESOLUTION CRYSTAL STRUCTURE OF THE CARBAMATE KINASE-LIKE CARBAMOYL PHOSPHATE SYNTHETASE FROM THE HYPERTHERMOPHILIC ARCHAEON PYROCOCCUS FURIOSUS, BOUND TO ADP, CONFIRMS THAT THIS THERMOESTABLE ENZYME IS A CARBAMATE KINASE, AND PROVIDES INSIGHTS INTO SUBSTRATE BINDING AND STABILITY IN CARBAMATE KINASES J.MOL.BIOL. v.299;463,2000	A	REGULATORY ADP BINDING RESIDUE	M - 274
1e19_A_274	1e19 RefS.RAMON-MAIQUES,A.MARINA,M.URIARTE,I.FITA,V.RUBIO. THE 1.5-A RESOLUTION CRYSTAL STRUCTURE OF THE CARBAMATE KINASE-LIKE CARBAMOYL PHOSPHATE SYNTHETASE FROM THE HYPERTHERMOPHILIC ARCHAEON PYROCOCCUS FURIOSUS, BOUND TO ADP, CONFIRMS THAT THIS THERMOESTABLE ENZYME IS A CARBAMATE KINASE, AND PROVIDES INSIGHTS INTO SUBSTRATE BINDING AND STABILITY IN CARBAMATE KINASES J.MOL.BIOL. v.299;463,2000	A	CATALYTIC RESIDUE	K - 277

Clusters included in this Subclass

CLUSTER: HE.3.7