3OID
Crystal Structure of Enoyl-ACP Reductases III (FabL) from B. subtilis (complex with NADP and TCL)
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004318 | molecular_function | enoyl-[acyl-carrier-protein] reductase (NADH) activity |
A | 0006633 | biological_process | fatty acid biosynthetic process |
A | 0016491 | molecular_function | oxidoreductase activity |
A | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
A | 0030497 | biological_process | fatty acid elongation |
A | 0050661 | molecular_function | NADP binding |
A | 0141148 | molecular_function | enoyl-[acyl-carrier-protein] reductase (NADPH) activity |
B | 0004318 | molecular_function | enoyl-[acyl-carrier-protein] reductase (NADH) activity |
B | 0006633 | biological_process | fatty acid biosynthetic process |
B | 0016491 | molecular_function | oxidoreductase activity |
B | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
B | 0030497 | biological_process | fatty acid elongation |
B | 0050661 | molecular_function | NADP binding |
B | 0141148 | molecular_function | enoyl-[acyl-carrier-protein] reductase (NADPH) activity |
C | 0004318 | molecular_function | enoyl-[acyl-carrier-protein] reductase (NADH) activity |
C | 0006633 | biological_process | fatty acid biosynthetic process |
C | 0016491 | molecular_function | oxidoreductase activity |
C | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
C | 0030497 | biological_process | fatty acid elongation |
C | 0050661 | molecular_function | NADP binding |
C | 0141148 | molecular_function | enoyl-[acyl-carrier-protein] reductase (NADPH) activity |
D | 0004318 | molecular_function | enoyl-[acyl-carrier-protein] reductase (NADH) activity |
D | 0006633 | biological_process | fatty acid biosynthetic process |
D | 0016491 | molecular_function | oxidoreductase activity |
D | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
D | 0030497 | biological_process | fatty acid elongation |
D | 0050661 | molecular_function | NADP binding |
D | 0141148 | molecular_function | enoyl-[acyl-carrier-protein] reductase (NADPH) activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE TCL A 601 |
Chain | Residue |
A | ALA91 |
A | SER92 |
A | GLY93 |
A | TYR151 |
A | ALA191 |
A | LEU192 |
A | HIS194 |
A | PHE195 |
A | NDP501 |
site_id | AC2 |
Number of Residues | 34 |
Details | BINDING SITE FOR RESIDUE NDP A 501 |
Chain | Residue |
A | GLY11 |
A | SER13 |
A | ARG14 |
A | GLY15 |
A | VAL16 |
A | ASN34 |
A | TYR35 |
A | ALA36 |
A | ARG37 |
A | SER38 |
A | ALA61 |
A | ASN62 |
A | VAL63 |
A | ASN89 |
A | ALA90 |
A | ALA91 |
A | ILE112 |
A | ILE139 |
A | SER140 |
A | SER141 |
A | LYS158 |
A | GLY184 |
A | GLY185 |
A | ALA186 |
A | ILE187 |
A | THR189 |
A | ALA191 |
A | LEU192 |
A | HOH270 |
A | HOH287 |
A | HOH316 |
A | HOH325 |
A | HOH478 |
A | TCL601 |
site_id | AC3 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE TCL B 603 |
Chain | Residue |
B | SER92 |
B | GLY93 |
B | TYR151 |
B | ALA191 |
B | LEU192 |
B | HIS194 |
B | PHE195 |
B | NDP503 |
site_id | AC4 |
Number of Residues | 34 |
Details | BINDING SITE FOR RESIDUE NDP B 503 |
Chain | Residue |
B | GLY11 |
B | SER13 |
B | ARG14 |
B | GLY15 |
B | VAL16 |
B | ASN34 |
B | ALA36 |
B | ARG37 |
B | SER38 |
B | ALA61 |
B | ASN62 |
B | VAL63 |
B | ASN89 |
B | ALA90 |
B | ALA91 |
B | ILE112 |
B | ILE139 |
B | SER140 |
B | SER141 |
B | LYS158 |
B | GLY184 |
B | GLY185 |
B | ALA186 |
B | ILE187 |
B | THR189 |
B | ALA191 |
B | HOH263 |
B | HOH278 |
B | HOH293 |
B | HOH442 |
B | HOH443 |
B | HOH446 |
B | HOH548 |
B | TCL603 |
site_id | AC5 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE TCL C 604 |
Chain | Residue |
C | ALA91 |
C | SER92 |
C | GLY93 |
C | TYR151 |
C | ALA191 |
C | HIS194 |
C | PHE195 |
C | NDP504 |
site_id | AC6 |
Number of Residues | 33 |
Details | BINDING SITE FOR RESIDUE NDP C 504 |
Chain | Residue |
C | ALA36 |
C | ARG37 |
C | SER38 |
C | ALA61 |
C | ASN62 |
C | VAL63 |
C | ASN89 |
C | ALA90 |
C | ALA91 |
C | ILE112 |
C | ILE139 |
C | SER140 |
C | SER141 |
C | LYS158 |
C | GLY184 |
C | GLY185 |
C | ALA186 |
C | ILE187 |
C | THR189 |
C | ALA191 |
C | HOH261 |
C | HOH281 |
C | HOH379 |
C | HOH380 |
C | HOH381 |
C | HOH432 |
C | TCL604 |
C | GLY11 |
C | SER13 |
C | ARG14 |
C | GLY15 |
C | VAL16 |
C | ASN34 |
site_id | AC7 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE TCL D 602 |
Chain | Residue |
D | SER92 |
D | GLY93 |
D | TYR151 |
D | ALA191 |
D | LEU192 |
D | PHE195 |
D | NDP502 |
site_id | AC8 |
Number of Residues | 34 |
Details | BINDING SITE FOR RESIDUE NDP D 502 |
Chain | Residue |
D | GLY11 |
D | SER13 |
D | ARG14 |
D | GLY15 |
D | VAL16 |
D | ASN34 |
D | ALA36 |
D | ARG37 |
D | SER38 |
D | ALA61 |
D | ASN62 |
D | VAL63 |
D | ASN89 |
D | ALA90 |
D | ALA91 |
D | ILE112 |
D | ILE139 |
D | SER140 |
D | SER141 |
D | LYS158 |
D | GLY184 |
D | GLY185 |
D | ALA186 |
D | ILE187 |
D | THR189 |
D | ALA191 |
D | HOH262 |
D | HOH288 |
D | HOH305 |
D | HOH326 |
D | HOH327 |
D | HOH328 |
D | HOH329 |
D | TCL602 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 8 |
Details | ACT_SITE: Proton acceptor => ECO:0000305|PubMed:21185310 |
Chain | Residue | Details |
A | TYR151 | |
A | LYS158 | |
B | TYR151 | |
B | LYS158 | |
C | TYR151 | |
C | LYS158 | |
D | TYR151 | |
D | LYS158 |
site_id | SWS_FT_FI2 |
Number of Residues | 24 |
Details | BINDING: BINDING => ECO:0000269|PubMed:21185310, ECO:0007744|PDB:3OID |
Chain | Residue | Details |
A | SER13 | |
B | ASN89 | |
B | LYS158 | |
B | ILE187 | |
C | SER13 | |
C | ALA36 | |
C | ASN62 | |
C | ASN89 | |
C | LYS158 | |
C | ILE187 | |
D | SER13 | |
A | ALA36 | |
D | ALA36 | |
D | ASN62 | |
D | ASN89 | |
D | LYS158 | |
D | ILE187 | |
A | ASN62 | |
A | ASN89 | |
A | LYS158 | |
A | ILE187 | |
B | SER13 | |
B | ALA36 | |
B | ASN62 |