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4OOK

Third Metal bound M.tuberculosis methionine aminopeptidase

Functional Information from GO Data
ChainGOidnamespacecontents
A0004177molecular_functionaminopeptidase activity
A0004239molecular_functioninitiator methionyl aminopeptidase activity
A0005506molecular_functioniron ion binding
A0005829cellular_componentcytosol
A0006508biological_processproteolysis
A0008235molecular_functionmetalloexopeptidase activity
A0016485biological_processprotein processing
A0046872molecular_functionmetal ion binding
A0050897molecular_functioncobalt ion binding
A0070006molecular_functionmetalloaminopeptidase activity
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CO A 301
ChainResidue
AASP131
AASP142
AGLU269
ACO302
AHOH401
AHOH430

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE CO A 302
ChainResidue
AGLU238
AGLU269
ACO301
AHOH401
AASP142
AHIS205
ATHR236

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CO A 303
ChainResidue
AHIS114
AHOH428
AHOH450

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE NA A 304
ChainResidue
AILE112
AMET240
ATHR265
AALA266
AHOH483

site_idAC5
Number of Residues3
DetailsBINDING SITE FOR RESIDUE NA A 305
ChainResidue
AMET50
AHIS140
AGLY141

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: BINDING => ECO:0000255|HAMAP-Rule:MF_01974, ECO:0000269|PubMed:15882055, ECO:0000269|PubMed:20038112, ECO:0000269|PubMed:21465667
ChainResidueDetails
AHIS114
AASP131
AASP142
AHIS205
AHIS212
AGLU238
AGLU269

227111

PDB entries from 2024-11-06

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