5OVK
Crystal structure MabA bound to NADPH from M. smegmatis
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004316 | molecular_function | 3-oxoacyl-[acyl-carrier-protein] reductase (NADPH) activity |
A | 0005576 | cellular_component | extracellular region |
A | 0006633 | biological_process | fatty acid biosynthetic process |
A | 0016491 | molecular_function | oxidoreductase activity |
A | 0018454 | molecular_function | acetoacetyl-CoA reductase activity |
A | 0030497 | biological_process | fatty acid elongation |
A | 0050661 | molecular_function | NADP binding |
B | 0004316 | molecular_function | 3-oxoacyl-[acyl-carrier-protein] reductase (NADPH) activity |
B | 0005576 | cellular_component | extracellular region |
B | 0006633 | biological_process | fatty acid biosynthetic process |
B | 0016491 | molecular_function | oxidoreductase activity |
B | 0018454 | molecular_function | acetoacetyl-CoA reductase activity |
B | 0030497 | biological_process | fatty acid elongation |
B | 0050661 | molecular_function | NADP binding |
C | 0004316 | molecular_function | 3-oxoacyl-[acyl-carrier-protein] reductase (NADPH) activity |
C | 0005576 | cellular_component | extracellular region |
C | 0006633 | biological_process | fatty acid biosynthetic process |
C | 0016491 | molecular_function | oxidoreductase activity |
C | 0018454 | molecular_function | acetoacetyl-CoA reductase activity |
C | 0030497 | biological_process | fatty acid elongation |
C | 0050661 | molecular_function | NADP binding |
D | 0004316 | molecular_function | 3-oxoacyl-[acyl-carrier-protein] reductase (NADPH) activity |
D | 0005576 | cellular_component | extracellular region |
D | 0006633 | biological_process | fatty acid biosynthetic process |
D | 0016491 | molecular_function | oxidoreductase activity |
D | 0018454 | molecular_function | acetoacetyl-CoA reductase activity |
D | 0030497 | biological_process | fatty acid elongation |
D | 0050661 | molecular_function | NADP binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 16 |
Details | binding site for residue NDP A 301 |
Chain | Residue |
A | GLY30 |
A | THR119 |
A | HOH403 |
A | HOH410 |
A | HOH424 |
A | HOH430 |
A | HOH436 |
A | HOH479 |
A | ASN32 |
A | ARG33 |
A | ARG55 |
A | CYS68 |
A | ASP69 |
A | VAL70 |
A | ALA97 |
A | GLY98 |
site_id | AC2 |
Number of Residues | 29 |
Details | binding site for residue NDP B 301 |
Chain | Residue |
B | GLY30 |
B | ASN32 |
B | ARG33 |
B | ILE35 |
B | ARG55 |
B | CYS68 |
B | ASP69 |
B | VAL70 |
B | ASN96 |
B | ALA97 |
B | GLY98 |
B | ILE99 |
B | THR119 |
B | ILE146 |
B | GLY147 |
B | TYR161 |
B | LYS165 |
B | PRO191 |
B | GLY192 |
B | ILE194 |
B | THR196 |
B | HOH405 |
B | HOH406 |
B | HOH424 |
B | HOH433 |
B | HOH474 |
B | HOH490 |
B | HOH493 |
B | HOH499 |
site_id | AC3 |
Number of Residues | 13 |
Details | binding site for residue NDP C 301 |
Chain | Residue |
C | GLY30 |
C | ASN32 |
C | ARG33 |
C | ILE35 |
C | ARG55 |
C | CYS68 |
C | ASP69 |
C | VAL70 |
C | ALA97 |
C | GLY98 |
C | THR119 |
C | HOH445 |
C | HOH465 |
site_id | AC4 |
Number of Residues | 15 |
Details | binding site for residue NDP D 301 |
Chain | Residue |
D | GLY30 |
D | ASN32 |
D | ARG33 |
D | ARG55 |
D | CYS68 |
D | ASP69 |
D | VAL70 |
D | ALA97 |
D | GLY98 |
D | THR119 |
D | GLU197 |
D | HOH422 |
D | HOH431 |
D | HOH491 |
D | HOH561 |
Functional Information from PROSITE/UniProt
site_id | PS00061 |
Number of Residues | 29 |
Details | ADH_SHORT Short-chain dehydrogenases/reductases family signature. SvsgmwgignQanYAAAKAGLiGMArSIS |
Chain | Residue | Details |
A | SER148-SER176 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 4 |
Details | ACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU10001 |
Chain | Residue | Details |
A | TYR161 | |
B | TYR161 | |
C | TYR161 | |
D | TYR161 |
site_id | SWS_FT_FI2 |
Number of Residues | 28 |
Details | BINDING: BINDING => ECO:0000269|PubMed:29717709 |
Chain | Residue | Details |
A | ASN32 | |
B | ASP69 | |
B | TYR161 | |
B | LYS165 | |
B | ILE194 | |
B | ARG205 | |
C | ASN32 | |
C | ARG55 | |
C | ASP69 | |
C | TYR161 | |
C | LYS165 | |
A | ARG55 | |
C | ILE194 | |
C | ARG205 | |
D | ASN32 | |
D | ARG55 | |
D | ASP69 | |
D | TYR161 | |
D | LYS165 | |
D | ILE194 | |
D | ARG205 | |
A | ASP69 | |
A | TYR161 | |
A | LYS165 | |
A | ILE194 | |
A | ARG205 | |
B | ASN32 | |
B | ARG55 |
site_id | SWS_FT_FI3 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000250|UniProtKB:P9WGT3 |
Chain | Residue | Details |
A | GLY98 | |
B | GLY98 | |
C | GLY98 | |
D | GLY98 |
site_id | SWS_FT_FI4 |
Number of Residues | 4 |
Details | SITE: Important for activity => ECO:0000250|UniProtKB:P9WGT3 |
Chain | Residue | Details |
A | SER148 | |
B | SER148 | |
C | SER148 | |
D | SER148 |