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4IF7

Mycobacterium Tuberculosis Methionine aminopeptidase Type 1c in complex with homocysteine-methyl disulfide

Functional Information from GO Data
ChainGOidnamespacecontents
A0004177molecular_functionaminopeptidase activity
A0004239molecular_functioninitiator methionyl aminopeptidase activity
A0005506molecular_functioniron ion binding
A0005829cellular_componentcytosol
A0006508biological_processproteolysis
A0008233molecular_functionpeptidase activity
A0016485biological_processprotein processing
A0016787molecular_functionhydrolase activity
A0046872molecular_functionmetal ion binding
A0050897molecular_functioncobalt ion binding
A0070006molecular_functionmetalloaminopeptidase activity
Functional Information from PDB Data
site_idAC1
Number of Residues7
DetailsBINDING SITE FOR RESIDUE CO A 401
ChainResidue
AASP142
AHIS205
ATHR236
AGLU238
AGLU269
ACO402
AHCM403

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CO A 402
ChainResidue
AGLU269
ACO401
AHCM403
AASP131
AASP142

site_idAC3
Number of Residues15
DetailsBINDING SITE FOR RESIDUE HCM A 403
ChainResidue
ATHR94
APHE100
AHIS114
AASP131
ATHR133
AASP142
AHIS205
APHE211
AHIS212
AGLU238
ATRP255
AGLU269
ACO401
ACO402
AHOH564

Functional Information from PROSITE/UniProt
site_idPS00680
Number of Residues19
DetailsMAP_1 Methionine aminopeptidase subfamily 1 signature. FtGHGIGttfHnglvVl.HY
ChainResidueDetails
APHE202-TYR220

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues7
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01974","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"15882055","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20038112","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"21465667","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

246704

PDB entries from 2025-12-24

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