3RMJ
Crystal structure of truncated alpha-Isopropylmalate Synthase from Neisseria meningitidis
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0019752 | biological_process | carboxylic acid metabolic process |
| A | 0046912 | molecular_function | acyltransferase activity, acyl groups converted into alkyl on transfer |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0019752 | biological_process | carboxylic acid metabolic process |
| B | 0046912 | molecular_function | acyltransferase activity, acyl groups converted into alkyl on transfer |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MN A 365 |
| Chain | Residue |
| A | ASP16 |
| A | HIS204 |
| A | HIS206 |
| A | ASN240 |
| A | HOH369 |
| A | HOH497 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE MG A 366 |
| Chain | Residue |
| A | HOH492 |
| A | HOH493 |
| A | HOH494 |
| A | HOH495 |
| A | ALA191 |
| A | ILE278 |
| A | HOH491 |
| site_id | AC3 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL A 367 |
| Chain | Residue |
| A | ARG15 |
| A | GLU143 |
| A | HOH450 |
| A | HOH469 |
| A | HOH471 |
| A | HOH496 |
| A | HOH532 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL A 368 |
| Chain | Residue |
| A | PRO94 |
| A | LYS95 |
| A | LYS96 |
| A | THR135 |
| A | ASP136 |
| A | HOH537 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MN B 365 |
| Chain | Residue |
| B | ASP16 |
| B | HIS204 |
| B | HIS206 |
| B | ASN240 |
| B | HOH370 |
| B | HOH421 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG B 366 |
| Chain | Residue |
| B | ALA24 |
| B | HOH479 |
| B | HOH480 |
| B | HOH481 |
| B | HOH482 |
| B | HOH483 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL B 367 |
| Chain | Residue |
| B | ARG15 |
| B | SER141 |
| B | GLU143 |
| B | HOH457 |
| B | HOH491 |
| B | HOH511 |
| site_id | AC8 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL B 368 |
| Chain | Residue |
| B | ARG6 |
| B | GLY41 |
| B | ASP43 |
| B | LYS69 |
| B | GLY262 |
| B | HOH447 |
| site_id | AC9 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL B 369 |
| Chain | Residue |
| B | PRO94 |
| B | LYS95 |
| B | LYS96 |
| B | THR135 |
| B | ASP136 |
| B | HOH463 |
Functional Information from PROSITE/UniProt
| site_id | PS00815 |
| Number of Residues | 17 |
| Details | AIPM_HOMOCIT_SYNTH_1 Alpha-isopropylmalate and homocitrate synthases signature 1. LRDGeQspgaAmtkeeK |
| Chain | Residue | Details |
| A | LEU14-LYS30 |
| site_id | PS00816 |
| Number of Residues | 14 |
| Details | AIPM_HOMOCIT_SYNTH_2 Alpha-isopropylmalate and homocitrate synthases signature 2. WsaHcHNDlGlAvA |
| Chain | Residue | Details |
| A | TRP201-ALA214 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 524 |
| Details | Domain: {"description":"Pyruvate carboxyltransferase","evidences":[{"source":"HAMAP-Rule","id":"MF_01025","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 8 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01025","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"22352945","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3RMJ","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
