1HZP
Crystal Structure of the Myobacterium Tuberculosis Beta-Ketoacyl-Acyl Carrier Protein Synthase III
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000062 | molecular_function | fatty-acyl-CoA binding |
| A | 0004315 | molecular_function | 3-oxoacyl-[acyl-carrier-protein] synthase activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0006633 | biological_process | fatty acid biosynthetic process |
| A | 0008610 | biological_process | lipid biosynthetic process |
| A | 0016746 | molecular_function | acyltransferase activity |
| A | 0030497 | biological_process | fatty acid elongation |
| A | 0033818 | molecular_function | beta-ketoacyl-acyl-carrier-protein synthase III activity |
| A | 0035336 | biological_process | long-chain fatty-acyl-CoA metabolic process |
| A | 0061990 | molecular_function | beta-ketodecanoyl-[acyl-carrier-protein] synthase activity |
| B | 0000062 | molecular_function | fatty-acyl-CoA binding |
| B | 0004315 | molecular_function | 3-oxoacyl-[acyl-carrier-protein] synthase activity |
| B | 0005515 | molecular_function | protein binding |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0006633 | biological_process | fatty acid biosynthetic process |
| B | 0008610 | biological_process | lipid biosynthetic process |
| B | 0016746 | molecular_function | acyltransferase activity |
| B | 0030497 | biological_process | fatty acid elongation |
| B | 0033818 | molecular_function | beta-ketoacyl-acyl-carrier-protein synthase III activity |
| B | 0035336 | biological_process | long-chain fatty-acyl-CoA metabolic process |
| B | 0061990 | molecular_function | beta-ketodecanoyl-[acyl-carrier-protein] synthase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE DAO A 408 |
| Chain | Residue |
| A | CYS112 |
| A | GLY305 |
| A | ILE189 |
| A | LEU207 |
| A | GLY209 |
| A | VAL212 |
| A | HIS244 |
| A | ALA246 |
| A | ASN274 |
| A | TYR304 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL A 400 |
| Chain | Residue |
| A | ASP222 |
| A | ARG225 |
| A | ARG226 |
| A | HOH652 |
| A | HOH835 |
| site_id | AC3 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL A 401 |
| Chain | Residue |
| A | ALA10 |
| A | ARG12 |
| A | ALA285 |
| A | GLU286 |
| A | THR289 |
| A | HOH557 |
| A | HOH590 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE GOL A 402 |
| Chain | Residue |
| A | TYR34 |
| A | GLY38 |
| A | SER248 |
| A | GLU252 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL A 403 |
| Chain | Residue |
| A | VAL255 |
| A | LEU260 |
| A | ARG261 |
| A | PRO262 |
| A | ALA263 |
| A | VAL265 |
| site_id | AC6 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE GOL A 404 |
| Chain | Residue |
| A | HOH557 |
| A | HOH775 |
| A | HOH856 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL B 406 |
| Chain | Residue |
| B | LEU207 |
| B | GLY209 |
| B | ALA246 |
| B | ASN274 |
| B | HOH742 |
| site_id | AC8 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL A 407 |
| Chain | Residue |
| A | ASP48 |
| A | SER50 |
| A | HOH573 |
| A | HOH714 |
| A | HOH888 |
| B | ASP194 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 6 |
| Details | ACT_SITE: ACT_SITE => ECO:0000255|HAMAP-Rule:MF_01815, ECO:0000305|PubMed:11278743, ECO:0000305|PubMed:16040614 |
| Chain | Residue | Details |
| A | CYS112 | |
| A | HIS244 | |
| A | ASN274 | |
| B | CYS112 | |
| B | HIS244 | |
| B | ASN274 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:15713483, ECO:0000305|PubMed:18096200, ECO:0007744|PDB:1U6S, ECO:0007744|PDB:2QX1 |
| Chain | Residue | Details |
| A | SER28 | |
| B | SER28 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:15713483, ECO:0000305|PubMed:11278743, ECO:0007744|PDB:1HZP, ECO:0007744|PDB:1U6S |
| Chain | Residue | Details |
| A | CYS112 | |
| B | CYS112 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000305|PubMed:11278743, ECO:0007744|PDB:1HZP |
| Chain | Residue | Details |
| A | ASN274 | |
| A | TYR304 | |
| B | ASN274 | |
| B | TYR304 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:15713483, ECO:0007744|PDB:1U6S |
| Chain | Residue | Details |
| A | ALA306 | |
| B | ALA306 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | MOD_RES: N-acetylthreonine => ECO:0007744|PubMed:21969609 |
| Chain | Residue | Details |
| A | THR-9 | |
| B | THR-9 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphothreonine => ECO:0000269|PubMed:19074144 |
| Chain | Residue | Details |
| A | THR35 | |
| B | THR35 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1cgk |
| Chain | Residue | Details |
| A | ASN274 | |
| A | CYS112 | |
| A | PHE157 | |
| A | HIS244 |
| site_id | CSA2 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1cgk |
| Chain | Residue | Details |
| B | ASN274 | |
| B | CYS112 | |
| B | PHE157 | |
| B | HIS244 |
