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1WKM

THE PRODUCT BOUND FORM OF THE MN(II)LOADED 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 Residues6
DetailsBINDING SITE FOR RESIDUE MN A 296
ChainResidue
AASP93
AHIS153
AGLU187
AGLU280
AMN297
AMET1298

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MN A 297
ChainResidue
AMN296
AMET1298
AASP82
AASP93
AGLU280

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MN B 296
ChainResidue
BASP82
BASP93
BGLU280
BMN297
BMET2298

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MN B 297
ChainResidue
BASP93
BHIS153
BGLU187
BGLU280
BMN296
BMET2298

site_idAC5
Number of Residues12
DetailsBINDING SITE FOR RESIDUE MET A 1298
ChainResidue
APHE50
AASN53
AHIS62
AASP82
AASP93
AHIS153
AHIS161
AGLU187
AILE205
AGLU280
AMN296
AMN297

site_idAC6
Number of Residues12
DetailsBINDING SITE FOR RESIDUE MET B 2298
ChainResidue
BPHE50
BASN53
BHIS62
BASP82
BASP93
BHIS153
BHIS161
BGLU187
BILE205
BGLU280
BMN296
BMN297

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_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

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

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PDB entries from 2024-05-01

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