2GEK
Crystal Structure of phosphatidylinositol mannosyltransferase (PimA) from Mycobacterium smegmatis in complex with GDP
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004377 | molecular_function | GDP-Man:Man3GlcNAc2-PP-Dol alpha-1,2-mannosyltransferase activity |
A | 0005886 | cellular_component | plasma membrane |
A | 0008654 | biological_process | phospholipid biosynthetic process |
A | 0009247 | biological_process | glycolipid biosynthetic process |
A | 0016757 | molecular_function | glycosyltransferase activity |
A | 0043750 | molecular_function | phosphatidylinositol alpha-mannosyltransferase activity |
A | 0046488 | biological_process | phosphatidylinositol metabolic process |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 13 |
Details | BINDING SITE FOR RESIDUE GDP A 2567 |
Chain | Residue |
A | PRO14 |
A | LYS256 |
A | ILE278 |
A | VAL279 |
A | GLU282 |
A | GLY15 |
A | GLY16 |
A | LEU194 |
A | LYS202 |
A | GLN250 |
A | VAL251 |
A | ASP252 |
A | ASP253 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 1 |
Details | BINDING: BINDING => ECO:0000305|PubMed:17510062 |
Chain | Residue | Details |
A | TYR9 |
site_id | SWS_FT_FI2 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000269|PubMed:17510062, ECO:0000269|PubMed:19520856 |
Chain | Residue | Details |
A | GLY16 | |
A | VAL251 | |
A | LYS256 | |
A | GLU282 |
site_id | SWS_FT_FI3 |
Number of Residues | 3 |
Details | BINDING: BINDING => ECO:0000305|PubMed:19520856 |
Chain | Residue | Details |
A | GLN18 | |
A | TYR62 | |
A | ARG68 |
site_id | SWS_FT_FI4 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000269|PubMed:17510062, ECO:0000305|PubMed:19520856 |
Chain | Residue | Details |
A | ARG196 | |
A | ARG201 |
site_id | SWS_FT_FI5 |
Number of Residues | 1 |
Details | BINDING: BINDING => ECO:0000269|PubMed:17510062 |
Chain | Residue | Details |
A | GLU274 |
site_id | SWS_FT_FI6 |
Number of Residues | 1 |
Details | SITE: Important for catalytic activity => ECO:0000269|PubMed:17510062 |
Chain | Residue | Details |
A | HIS118 |