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6M00

crystal structure of Methionine aminopeptidase from 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_idAC1
Number of Residues5
Detailsbinding site for residue CO A 301
ChainResidue
AASP82
AASP93
AGLU187
AGLU280
ACO302

site_idAC2
Number of Residues5
Detailsbinding site for residue CO A 302
ChainResidue
ACO301
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_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 2024-07-17

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