4JN6
Crystal Structure of the Aldolase-Dehydrogenase Complex from Mycobacterium tuberculosis HRv37
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0003852 | molecular_function | 2-isopropylmalate synthase activity |
| A | 0008701 | molecular_function | 4-hydroxy-2-oxovalerate aldolase activity |
| A | 0009056 | biological_process | catabolic process |
| A | 0009098 | biological_process | L-leucine biosynthetic process |
| A | 0009274 | cellular_component | peptidoglycan-based cell wall |
| A | 0016829 | molecular_function | lyase activity |
| A | 0016833 | molecular_function | oxo-acid-lyase activity |
| A | 0030145 | molecular_function | manganese ion binding |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0008774 | molecular_function | acetaldehyde dehydrogenase (acetylating) activity |
| B | 0009056 | biological_process | catabolic process |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0016620 | molecular_function | oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor |
| B | 0051287 | molecular_function | NAD binding |
| C | 0003824 | molecular_function | catalytic activity |
| C | 0003852 | molecular_function | 2-isopropylmalate synthase activity |
| C | 0008701 | molecular_function | 4-hydroxy-2-oxovalerate aldolase activity |
| C | 0009056 | biological_process | catabolic process |
| C | 0009098 | biological_process | L-leucine biosynthetic process |
| C | 0009274 | cellular_component | peptidoglycan-based cell wall |
| C | 0016829 | molecular_function | lyase activity |
| C | 0016833 | molecular_function | oxo-acid-lyase activity |
| C | 0030145 | molecular_function | manganese ion binding |
| C | 0046872 | molecular_function | metal ion binding |
| D | 0008774 | molecular_function | acetaldehyde dehydrogenase (acetylating) activity |
| D | 0009056 | biological_process | catabolic process |
| D | 0016491 | molecular_function | oxidoreductase activity |
| D | 0016620 | molecular_function | oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor |
| D | 0051287 | molecular_function | NAD binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE OXL A 401 |
| Chain | Residue |
| A | ARG15 |
| A | MN402 |
| A | HOH578 |
| A | HOH595 |
| A | ASP16 |
| A | PHE137 |
| A | MET139 |
| A | VAL167 |
| A | SER169 |
| A | HIS198 |
| A | HIS200 |
| A | TYR289 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MN A 402 |
| Chain | Residue |
| A | ASP16 |
| A | HIS198 |
| A | HIS200 |
| A | OXL401 |
| A | HOH578 |
| site_id | AC3 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE OXL C 401 |
| Chain | Residue |
| C | ARG15 |
| C | ASP16 |
| C | PHE137 |
| C | MET139 |
| C | VAL167 |
| C | SER169 |
| C | HIS198 |
| C | HIS200 |
| C | TYR289 |
| C | MN403 |
| C | HOH540 |
| C | HOH606 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE NA C 402 |
| Chain | Residue |
| C | HIS19 |
| C | HIS23 |
| C | TYR60 |
| C | HIS295 |
| C | HOH512 |
| C | HOH515 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MN C 403 |
| Chain | Residue |
| C | ASP16 |
| C | HIS198 |
| C | HIS200 |
| C | OXL401 |
| C | HOH540 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 504 |
| Details | Domain: {"description":"Pyruvate carboxyltransferase","evidences":[{"source":"PROSITE-ProRule","id":"PRU01151","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"HAMAP-Rule","id":"MF_01656","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 6 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01656","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"23614353","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01656","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"23614353","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01656","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | Site: {"description":"Transition state stabilizer","evidences":[{"source":"HAMAP-Rule","id":"MF_01656","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Acyl-thioester intermediate","evidences":[{"source":"HAMAP-Rule","id":"MF_01657","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 24 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01657","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
