4R3U
Crystal structure of 2-Hydroxyisobutyryl-CoA Mutase
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0004494 | molecular_function | methylmalonyl-CoA mutase activity |
| A | 0016853 | molecular_function | isomerase activity |
| A | 0016866 | molecular_function | intramolecular transferase activity |
| A | 0031419 | molecular_function | cobalamin binding |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0004494 | molecular_function | methylmalonyl-CoA mutase activity |
| B | 0016853 | molecular_function | isomerase activity |
| B | 0016866 | molecular_function | intramolecular transferase activity |
| B | 0031419 | molecular_function | cobalamin binding |
| C | 0016853 | molecular_function | isomerase activity |
| C | 0031419 | molecular_function | cobalamin binding |
| C | 0046872 | molecular_function | metal ion binding |
| D | 0016853 | molecular_function | isomerase activity |
| D | 0031419 | molecular_function | cobalamin binding |
| D | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 42 |
| Details | BINDING SITE FOR RESIDUE 3HC A 801 |
| Chain | Residue |
| A | PHE27 |
| A | SER115 |
| A | ASP117 |
| A | SER165 |
| A | THR167 |
| A | THR196 |
| A | GLN198 |
| A | GLN208 |
| A | ARG235 |
| A | ASN237 |
| A | ASN240 |
| A | TYR76 |
| A | TYR244 |
| A | HIS245 |
| A | ARG284 |
| A | ALA286 |
| A | PHE288 |
| A | ARG328 |
| A | PHE329 |
| A | HIS330 |
| A | GLN332 |
| A | GLN363 |
| A | THR78 |
| A | SER364 |
| A | 5AD803 |
| A | HOH911 |
| A | HOH917 |
| A | HOH939 |
| A | HOH945 |
| A | HOH977 |
| A | HOH999 |
| A | HOH1006 |
| A | HOH1009 |
| A | MET79 |
| A | HOH1021 |
| A | HOH1054 |
| C | B12800 |
| A | SER82 |
| A | ARG83 |
| A | THR86 |
| A | ARG88 |
| A | ILE90 |
| site_id | AC2 |
| Number of Residues | 41 |
| Details | BINDING SITE FOR RESIDUE 3KK A 802 |
| Chain | Residue |
| A | PHE27 |
| A | TYR76 |
| A | THR78 |
| A | MET79 |
| A | SER82 |
| A | ARG83 |
| A | THR86 |
| A | ARG88 |
| A | ILE90 |
| A | SER115 |
| A | ASP117 |
| A | SER165 |
| A | THR167 |
| A | THR196 |
| A | GLN198 |
| A | GLN208 |
| A | ARG235 |
| A | ASN237 |
| A | ASN240 |
| A | TYR244 |
| A | HIS245 |
| A | ARG284 |
| A | ALA286 |
| A | PHE288 |
| A | ARG328 |
| A | PHE329 |
| A | HIS330 |
| A | GLN332 |
| A | GLN363 |
| A | SER364 |
| A | 5AD803 |
| A | HOH911 |
| A | HOH917 |
| A | HOH939 |
| A | HOH945 |
| A | HOH977 |
| A | HOH999 |
| A | HOH1006 |
| A | HOH1009 |
| A | HOH1021 |
| C | B12800 |
| site_id | AC3 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE 5AD A 803 |
| Chain | Residue |
| A | HOH1053 |
| A | HOH1054 |
| A | HOH1056 |
| A | HOH1057 |
| C | B12800 |
| C | HOH938 |
| A | ILE90 |
| A | GLY92 |
| A | ASP117 |
| A | GLU140 |
| A | TYR244 |
| A | GLN332 |
| A | ALA335 |
| A | ASN368 |
| A | GLU372 |
| A | ILE376 |
| A | PRO377 |
| A | 3HC801 |
| A | 3KK802 |
| A | HOH923 |
| A | HOH978 |
| A | HOH1052 |
| site_id | AC4 |
| Number of Residues | 32 |
| Details | BINDING SITE FOR RESIDUE 3HC B 801 |
| Chain | Residue |
| B | PHE27 |
| B | ALA31 |
| B | TYR76 |
| B | THR78 |
| B | MET79 |
| B | SER82 |
| B | ARG83 |
| B | THR86 |
| B | ARG88 |
| B | ILE90 |
| B | SER115 |
| B | ASP117 |
| B | SER165 |
| B | THR167 |
| B | THR196 |
| B | GLN198 |
| B | GLN208 |
| B | ARG235 |
| B | ASN237 |
| B | ASN240 |
| B | TYR244 |
| B | HIS245 |
| B | ARG284 |
| B | ALA286 |
| B | PHE288 |
| B | ARG328 |
| B | PHE329 |
| B | HIS330 |
| B | GLN332 |
| B | GLN363 |
| B | SER364 |
| D | B12800 |
| site_id | AC5 |
| Number of Residues | 31 |
| Details | BINDING SITE FOR RESIDUE 3KK B 802 |
| Chain | Residue |
| B | PHE27 |
| B | TYR76 |
| B | THR78 |
| B | MET79 |
| B | SER82 |
| B | ARG83 |
| B | THR86 |
| B | ARG88 |
| B | ILE90 |
| B | SER115 |
| B | ASP117 |
| B | SER165 |
| B | THR167 |
| B | THR196 |
| B | GLN198 |
| B | GLN208 |
| B | ARG235 |
| B | ASN237 |
| B | ASN240 |
| B | TYR244 |
| B | HIS245 |
| B | ARG284 |
| B | ALA286 |
| B | PHE288 |
| B | ARG328 |
| B | PHE329 |
| B | HIS330 |
| B | GLN332 |
| B | GLN363 |
| B | SER364 |
| D | B12800 |
| site_id | AC6 |
| Number of Residues | 47 |
| Details | BINDING SITE FOR RESIDUE B12 C 800 |
| Chain | Residue |
| A | ASP117 |
| A | PHE118 |
| A | MET120 |
| A | LEU123 |
| A | GLU140 |
| A | ALA207 |
| A | GLN208 |
| A | GLU210 |
| A | GLU248 |
| A | ALA249 |
| A | ALA335 |
| A | GLU372 |
| A | ALA373 |
| A | ALA375 |
| A | ILE376 |
| A | 3HC801 |
| A | 3KK802 |
| A | 5AD803 |
| A | HOH903 |
| A | HOH910 |
| C | GLY17 |
| C | HIS18 |
| C | ASP19 |
| C | ARG20 |
| C | GLY21 |
| C | VAL25 |
| C | GLY61 |
| C | VAL62 |
| C | SER63 |
| C | LEU65 |
| C | GLY67 |
| C | ILE91 |
| C | ALA92 |
| C | GLY93 |
| C | GLY94 |
| C | LEU113 |
| C | LEU114 |
| C | GLN115 |
| C | THR117 |
| C | ILE122 |
| C | HOH904 |
| C | HOH905 |
| C | HOH907 |
| C | HOH910 |
| C | HOH922 |
| C | HOH936 |
| C | HOH938 |
| site_id | AC7 |
| Number of Residues | 37 |
| Details | BINDING SITE FOR RESIDUE B12 D 800 |
| Chain | Residue |
| B | ASP117 |
| B | PHE118 |
| B | MET120 |
| B | LEU123 |
| B | GLU140 |
| B | ALA207 |
| B | GLN208 |
| B | GLU210 |
| B | GLU248 |
| B | ALA249 |
| B | ALA335 |
| B | GLU372 |
| B | ALA373 |
| B | ALA375 |
| B | ILE376 |
| B | 3HC801 |
| B | 3KK802 |
| D | GLY17 |
| D | HIS18 |
| D | ASP19 |
| D | ARG20 |
| D | GLY21 |
| D | VAL25 |
| D | GLY61 |
| D | VAL62 |
| D | SER63 |
| D | LEU65 |
| D | GLY67 |
| D | ILE91 |
| D | GLY93 |
| D | GLY94 |
| D | LEU113 |
| D | LEU114 |
| D | GLN115 |
| D | THR117 |
| D | ILE122 |
| D | HOH901 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 24 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"25720495","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4R3U","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Site: {"description":"Important for the stereospecificity of catalysis","evidences":[{"source":"PubMed","id":"25720495","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 128 |
| Details | Domain: {"description":"B12-binding","evidences":[{"source":"PROSITE-ProRule","id":"PRU00666","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Binding site: {"description":"axial binding residue","evidences":[{"source":"PubMed","id":"25720495","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4R3U","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
