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2GEK

Crystal Structure of phosphatidylinositol mannosyltransferase (PimA) from Mycobacterium smegmatis in complex with GDP

Functional Information from GO Data
ChainGOidnamespacecontents
A0004377molecular_functionGDP-Man:Man3GlcNAc2-PP-Dol alpha-1,2-mannosyltransferase activity
A0005886cellular_componentplasma membrane
A0008654biological_processphospholipid biosynthetic process
A0009247biological_processglycolipid biosynthetic process
A0016757molecular_functionglycosyltransferase activity
A0043750molecular_functionphosphatidylinositol alpha-mannosyltransferase activity
A0046488biological_processphosphatidylinositol metabolic process
Functional Information from PDB Data
site_idAC1
Number of Residues13
DetailsBINDING SITE FOR RESIDUE GDP A 2567
ChainResidue
APRO14
ALYS256
AILE278
AVAL279
AGLU282
AGLY15
AGLY16
ALEU194
ALYS202
AGLN250
AVAL251
AASP252
AASP253

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsBINDING: BINDING => ECO:0000305|PubMed:17510062
ChainResidueDetails
ATYR9

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:17510062, ECO:0000269|PubMed:19520856
ChainResidueDetails
AGLY16
AVAL251
ALYS256
AGLU282

site_idSWS_FT_FI3
Number of Residues3
DetailsBINDING: BINDING => ECO:0000305|PubMed:19520856
ChainResidueDetails
AGLN18
ATYR62
AARG68

site_idSWS_FT_FI4
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:17510062, ECO:0000305|PubMed:19520856
ChainResidueDetails
AARG196
AARG201

site_idSWS_FT_FI5
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:17510062
ChainResidueDetails
AGLU274

site_idSWS_FT_FI6
Number of Residues1
DetailsSITE: Important for catalytic activity => ECO:0000269|PubMed:17510062
ChainResidueDetails
AHIS118

227344

PDB entries from 2024-11-13

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