2AJ9
X-ray crystal structure of W42A,R161A double mutant of Mycobacterium tuberculosis beta-ketoacyl-ACP 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 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 | CYS122 | |
| A | HIS258 | |
| A | ASN289 | |
| B | CYS122 | |
| B | HIS258 | |
| B | ASN289 |
| 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 | SER38 | |
| B | SER38 |
| 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 | CYS122 | |
| B | CYS122 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000305|PubMed:11278743, ECO:0007744|PDB:1HZP |
| Chain | Residue | Details |
| A | ASN289 | |
| A | TYR319 | |
| B | ASN289 | |
| B | TYR319 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:15713483, ECO:0007744|PDB:1U6S |
| Chain | Residue | Details |
| A | ALA321 | |
| B | ALA321 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | MOD_RES: N-acetylthreonine => ECO:0007744|PubMed:21969609 |
| Chain | Residue | Details |
| A | THR2 | |
| B | THR2 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphothreonine => ECO:0000269|PubMed:19074144 |
| Chain | Residue | Details |
| A | THR45 | |
| B | THR45 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1cgk |
| Chain | Residue | Details |
| A | CYS122 | |
| A | HIS258 | |
| A | ASN289 | |
| A | PHE167 |
| site_id | CSA2 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1cgk |
| Chain | Residue | Details |
| B | CYS122 | |
| B | HIS258 | |
| B | ASN289 | |
| B | PHE167 |
