Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

1XGS

METHIONINE AMINOPEPTIDASE FROM HYPERTHERMOPHILE PYROCOCCUS FURIOSUS

Functional Information from GO Data
ChainGOidnamespacecontents
A0004177molecular_functionaminopeptidase activity
A0004239molecular_functioninitiator methionyl aminopeptidase activity
A0006508biological_processproteolysis
A0046872molecular_functionmetal ion binding
A0070006molecular_functionmetalloaminopeptidase activity
B0004177molecular_functionaminopeptidase activity
B0004239molecular_functioninitiator methionyl aminopeptidase activity
B0006508biological_processproteolysis
B0046872molecular_functionmetal ion binding
B0070006molecular_functionmetalloaminopeptidase activity
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CO A 296
ChainResidue
AASP93
AHIS153
AGLU187
AGLU280
ACO297
AHOH298

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CO A 297
ChainResidue
AASP82
AASP93
AGLU280
ACO296
AHOH298

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CO B 296
ChainResidue
BASP93
BHIS153
BGLU187
BGLU280
BCO297
BHOH301

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CO B 297
ChainResidue
BASP82
BASP93
BGLU280
BCO296
BHOH301

site_idACA
Number of Residues8
DetailsSIDE CHAINS OF FIVE AMINO ACID RESIDUES ASP 82, ASP 93, HIS 153, GLU 187, GLU 280, TWO COBALT IONS SEPARATED BY 3.1 ANGSTROM, AND A BRIDGING WATER MOLECULE HOH 1 BOUND TO BOTH COBALT IONS FORM AN ACTIVE SITE OF MOLECULE IN CHAIN A.
ChainResidue
AASP82
AASP93
AHIS153
AGLU187
AGLU280
ACO296
ACO297
AHOH307

site_idACB
Number of Residues8
DetailsSIDE CHAINS OF FIVE AMINO ACID RESIDUES ASP 82, ASP 93, HIS 153, GLU 187, GLU 280, TWO COBALT IONS SEPARATED BY 3.1 ANGSTROM, AND A BRIDGING WATER MOLECULE HOH 1 BOUND TO BOTH COBALT IONS FORM AN ACTIVE SITE OF MOLECULE IN CHAIN B.
ChainResidue
BASP93
BHIS153
BGLU187
BGLU280
BCO296
BCO297
BHOH310
BASP82

Functional Information from PROSITE/UniProt
site_idPS01202
Number of Residues17
DetailsMAP_2 Methionine aminopeptidase subfamily 2 signature. DYlKIDvGvHIDGfiaD
ChainResidueDetails
AASP77-ASP93

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01975
ChainResidueDetails
AHIS62
BHIS62

site_idSWS_FT_FI2
Number of Residues12
DetailsBINDING:
ChainResidueDetails
AASP82
BHIS161
BGLU187
BGLU280
AASP93
AHIS153
AHIS161
AGLU187
AGLU280
BASP82
BASP93
BHIS153

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1a16
ChainResidueDetails
AGLU187
ASER165

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1a16
ChainResidueDetails
BGLU187
BSER165

site_idCSA3
Number of Residues1
DetailsAnnotated By Reference To The Literature 1a16
ChainResidueDetails
AGLU187

site_idCSA4
Number of Residues1
DetailsAnnotated By Reference To The Literature 1a16
ChainResidueDetails
BGLU187

site_idMCSA1
Number of Residues6
DetailsM-CSA 917
ChainResidueDetails
AASP82metal ligand
AASP93metal ligand
AHIS153metal ligand
AHIS161electrostatic stabiliser
AGLU187metal ligand, proton acceptor, proton donor
AGLU280metal ligand

site_idMCSA2
Number of Residues6
DetailsM-CSA 917
ChainResidueDetails
BASP82metal ligand
BASP93metal ligand
BHIS153metal ligand
BHIS161electrostatic stabiliser
BGLU187metal ligand, proton acceptor, proton donor
BGLU280metal ligand

222415

PDB entries from 2024-07-10

PDB statisticsPDBj update infoContact PDBjnumon