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1XGN

METHIONINE AMINOPEPTIDASE FROM HYPERTHERMOPHILE PYROCOCCUS FURIOSUS

Functional Information from GO Data
ChainGOidnamespacecontents
A0004177molecular_functionaminopeptidase activity
A0004239molecular_functioninitiator methionyl aminopeptidase activity
A0005737cellular_componentcytoplasm
A0006508biological_processproteolysis
A0008235molecular_functionmetalloexopeptidase activity
A0046872molecular_functionmetal ion binding
A0070006molecular_functionmetalloaminopeptidase activity
B0004177molecular_functionaminopeptidase activity
B0004239molecular_functioninitiator methionyl aminopeptidase activity
B0005737cellular_componentcytoplasm
B0006508biological_processproteolysis
B0008235molecular_functionmetalloexopeptidase activity
B0046872molecular_functionmetal ion binding
B0070006molecular_functionmetalloaminopeptidase activity
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CO A 296
ChainResidue
AASP93
AHIS153
AGLU187
AGLU280
ACO297

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CO A 297
ChainResidue
AASP82
AASP93
AGLU280
ACO296

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CO B 296
ChainResidue
BASP93
BHIS153
BGLU187
BGLU280
BCO297

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CO B 297
ChainResidue
BASP82
BASP93
BGLU280
BCO296

site_idACA
Number of Residues7
DetailsSIDE CHAINS OF FIVE AMINO ACID RESIDUES ASP 82, ASP 93, HIS 153, GLU 187, GLU 280, AND TWO COBALT IONS FORM AN ACTIVE SITE OF MOLECULE IN CHAIN A.
ChainResidue
AASP82
AASP93
AHIS153
AGLU187
AGLU280
ACO296
ACO297

site_idACB
Number of Residues7
DetailsSIDE CHAINS OF FIVE AMINO ACID RESIDUES ASP 82, ASP 93, HIS 153, GLU 187, GLU 280, AND TWO COBALT IONS FORM AN ACTIVE SITE OF MOLECULE IN CHAIN B.
ChainResidue
BHIS153
BGLU187
BGLU280
BCO296
BCO297
BASP82
BASP93

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
BASP82
BASP93
BHIS153
BHIS161
BGLU187
BGLU280
AASP82
AASP93
AHIS153
AHIS161
AGLU187
AGLU280

Catalytic Information from CSA
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

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PDB entries from 2024-05-29

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