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3ROR

Crystal structure of C105S mutant of Mycobacterium 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
A0046914molecular_functiontransition metal 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 290
ChainResidue
AASP142
AHIS205
ATHR236
AGLU238
AGLU269
ACO291
AHOH302

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CO A 291
ChainResidue
AGLU269
AHOH286
ACO290
AHOH302
AASP131
AASP142

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE K A 295
ChainResidue
ASER107
AASN109
AVAL111
ATHR265
AHOH297

site_idAC4
Number of Residues2
DetailsBINDING SITE FOR RESIDUE BME A 300
ChainResidue
AHIS270
ACYS284

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
AASP131
AASP142
AHIS205
AHIS212
AGLU238
AGLU269
AHIS114

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PDB entries from 2024-06-12

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