2XIQ
Crystal structure of human methylmalonyl-CoA mutase in complex with adenosylcobalamin and malonyl-CoA
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0003924 | molecular_function | GTPase activity |
| A | 0004494 | molecular_function | methylmalonyl-CoA mutase activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005739 | cellular_component | mitochondrion |
| A | 0005759 | cellular_component | mitochondrial matrix |
| A | 0006790 | biological_process | sulfur compound metabolic process |
| A | 0016853 | molecular_function | isomerase activity |
| A | 0016866 | molecular_function | intramolecular transferase activity |
| A | 0019678 | biological_process | propionate metabolic process, methylmalonyl pathway |
| A | 0031419 | molecular_function | cobalamin binding |
| A | 0042802 | molecular_function | identical protein binding |
| A | 0042803 | molecular_function | protein homodimerization activity |
| A | 0043547 | biological_process | positive regulation of GTPase activity |
| A | 0044281 | biological_process | small molecule metabolic process |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0050667 | biological_process | homocysteine metabolic process |
| A | 0072341 | molecular_function | modified amino acid binding |
| A | 1901290 | biological_process | succinyl-CoA biosynthetic process |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0003924 | molecular_function | GTPase activity |
| B | 0004494 | molecular_function | methylmalonyl-CoA mutase activity |
| B | 0005515 | molecular_function | protein binding |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005739 | cellular_component | mitochondrion |
| B | 0005759 | cellular_component | mitochondrial matrix |
| B | 0006790 | biological_process | sulfur compound metabolic process |
| B | 0016853 | molecular_function | isomerase activity |
| B | 0016866 | molecular_function | intramolecular transferase activity |
| B | 0019678 | biological_process | propionate metabolic process, methylmalonyl pathway |
| B | 0031419 | molecular_function | cobalamin binding |
| B | 0042802 | molecular_function | identical protein binding |
| B | 0042803 | molecular_function | protein homodimerization activity |
| B | 0043547 | biological_process | positive regulation of GTPase activity |
| B | 0044281 | biological_process | small molecule metabolic process |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0050667 | biological_process | homocysteine metabolic process |
| B | 0072341 | molecular_function | modified amino acid binding |
| B | 1901290 | biological_process | succinyl-CoA biosynthetic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 45 |
| Details | BINDING SITE FOR RESIDUE B12 A 3001 |
| Chain | Residue |
| A | TYR110 |
| A | HIS265 |
| A | GLU268 |
| A | GLY355 |
| A | TRP356 |
| A | LEU358 |
| A | GLU392 |
| A | GLY395 |
| A | LEU396 |
| A | GLN476 |
| A | GLY626 |
| A | PHE138 |
| A | HIS627 |
| A | ASP628 |
| A | ARG629 |
| A | GLY630 |
| A | ILE634 |
| A | GLY670 |
| A | SER672 |
| A | LEU674 |
| A | ALA676 |
| A | GLY702 |
| A | LEU140 |
| A | GLY703 |
| A | VAL704 |
| A | PHE722 |
| A | GLY723 |
| A | PRO724 |
| A | THR726 |
| A | HOH2058 |
| A | HOH2102 |
| A | HOH2405 |
| A | HOH2488 |
| A | HIS143 |
| A | HOH2489 |
| A | HOH2490 |
| A | HOH2491 |
| A | HOH2492 |
| A | 5AD4001 |
| A | MLC5001 |
| A | ALA160 |
| A | VAL227 |
| A | ARG228 |
| A | THR230 |
| A | TYR264 |
| site_id | AC2 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE 5AD A 4001 |
| Chain | Residue |
| A | TYR110 |
| A | GLY112 |
| A | ALA137 |
| A | ALA160 |
| A | TYR264 |
| A | GLN352 |
| A | GLY355 |
| A | ASN388 |
| A | GLU392 |
| A | LEU396 |
| A | PRO397 |
| A | HOH2493 |
| A | HOH2494 |
| A | B123001 |
| A | MLC5001 |
| site_id | AC3 |
| Number of Residues | 40 |
| Details | BINDING SITE FOR RESIDUE MLC A 5001 |
| Chain | Residue |
| B | GLN50 |
| A | TYR96 |
| A | THR98 |
| A | MET99 |
| A | ARG103 |
| A | THR106 |
| A | ARG108 |
| A | TYR110 |
| A | SER135 |
| A | SER185 |
| A | THR187 |
| A | THR216 |
| A | GLN218 |
| A | ARG228 |
| A | LYS255 |
| A | ASN257 |
| A | HIS265 |
| A | ARG304 |
| A | SER306 |
| A | PHE308 |
| A | ARG348 |
| A | ALA349 |
| A | HIS350 |
| A | GLN352 |
| A | GLN383 |
| A | HOH2053 |
| A | HOH2075 |
| A | HOH2135 |
| A | HOH2159 |
| A | HOH2189 |
| A | HOH2479 |
| A | HOH2480 |
| A | HOH2481 |
| A | HOH2482 |
| A | HOH2483 |
| A | HOH2484 |
| A | HOH2485 |
| A | HOH2486 |
| A | B123001 |
| A | 5AD4001 |
| site_id | AC4 |
| Number of Residues | 43 |
| Details | BINDING SITE FOR RESIDUE B12 B 3001 |
| Chain | Residue |
| B | TYR110 |
| B | PHE138 |
| B | LEU140 |
| B | HIS143 |
| B | ALA160 |
| B | VAL227 |
| B | ARG228 |
| B | THR230 |
| B | TYR264 |
| B | GLU268 |
| B | GLY355 |
| B | TRP356 |
| B | LEU358 |
| B | GLU392 |
| B | GLY395 |
| B | LEU396 |
| B | GLN476 |
| B | GLY626 |
| B | HIS627 |
| B | ASP628 |
| B | ARG629 |
| B | GLY630 |
| B | ILE634 |
| B | GLY670 |
| B | SER672 |
| B | LEU674 |
| B | ALA676 |
| B | GLY702 |
| B | GLY703 |
| B | VAL704 |
| B | PHE722 |
| B | GLY723 |
| B | THR726 |
| B | HOH2077 |
| B | HOH2132 |
| B | HOH2526 |
| B | HOH2606 |
| B | HOH2607 |
| B | HOH2608 |
| B | HOH2609 |
| B | HOH2610 |
| B | 5AD4001 |
| B | MLC5001 |
| site_id | AC5 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE 5AD B 4001 |
| Chain | Residue |
| B | TYR110 |
| B | GLY112 |
| B | ALA137 |
| B | ALA160 |
| B | TYR264 |
| B | GLN352 |
| B | ASN388 |
| B | GLU392 |
| B | LEU396 |
| B | PRO397 |
| B | HOH2308 |
| B | HOH2612 |
| B | B123001 |
| B | MLC5001 |
| site_id | AC6 |
| Number of Residues | 40 |
| Details | BINDING SITE FOR RESIDUE MLC B 5001 |
| Chain | Residue |
| A | GLN50 |
| B | TYR96 |
| B | THR98 |
| B | MET99 |
| B | PHE102 |
| B | ARG103 |
| B | THR106 |
| B | ARG108 |
| B | TYR110 |
| B | SER185 |
| B | THR187 |
| B | THR216 |
| B | GLN218 |
| B | ARG228 |
| B | LYS255 |
| B | ASN257 |
| B | HIS265 |
| B | ARG304 |
| B | SER306 |
| B | PHE308 |
| B | ARG348 |
| B | ALA349 |
| B | HIS350 |
| B | GLN352 |
| B | GLN383 |
| B | SER384 |
| B | HOH2069 |
| B | HOH2070 |
| B | HOH2186 |
| B | HOH2229 |
| B | HOH2598 |
| B | HOH2599 |
| B | HOH2600 |
| B | HOH2601 |
| B | HOH2602 |
| B | HOH2603 |
| B | HOH2604 |
| B | HOH2605 |
| B | B123001 |
| B | 5AD4001 |
Functional Information from PROSITE/UniProt
| site_id | PS00544 |
| Number of Residues | 26 |
| Details | METMALONYL_COA_MUTASE Methylmalonyl-CoA mutase signature. RIARNTqiIIqEEsgipKvaDPwGGS |
| Chain | Residue | Details |
| A | ARG403-SER428 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 264 |
| Details | Domain: {"description":"B12-binding","evidences":[{"source":"PROSITE-ProRule","id":"PRU00666","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 30 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"20876572","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Binding site: {"description":"axial binding residue","evidences":[{"source":"PubMed","id":"20876572","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 8 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P16332","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 4 |
| Details | Modified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"P16332","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
