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1XGO

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
Functional Information from PDB Data
site_idAC
Number of Residues5
DetailsSIDE CHAINS OF FIVE AMINO ACID RESIDUES ASP 82, ASP 93, HIS 153, GLU 187, AND GLU 280, FORM A SITE FOR BINDING OF TWO COBALT IONS.
ChainResidue
AASP82
AASP93
AHIS153
AGLU187
AGLU280

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 Residues1
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01975
ChainResidueDetails
AHIS62

site_idSWS_FT_FI2
Number of Residues6
DetailsBINDING:
ChainResidueDetails
AASP82
AASP93
AHIS153
AHIS161
AGLU187
AGLU280

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

site_idCSA2
Number of Residues1
DetailsAnnotated By Reference To The Literature 1a16
ChainResidueDetails
AGLU187

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

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PDB entries from 2024-07-10

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