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 | 0009791 | biological_process | post-embryonic development |
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 | 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 | 0009791 | biological_process | post-embryonic development |
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 | 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 | 16 |
Details | BINDING: BINDING => ECO:0000269|PubMed:20876572 |
Chain | Residue | Details |
A | GLN50 | |
B | TYR96 | |
B | THR106 | |
B | THR216 | |
B | ARG228 | |
B | LYS255 | |
B | HIS265 | |
B | ARG304 | |
A | TYR96 | |
A | THR106 | |
A | THR216 | |
A | ARG228 | |
A | LYS255 | |
A | HIS265 | |
A | ARG304 | |
B | GLN50 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | BINDING: axial binding residue => ECO:0000269|PubMed:20876572 |
Chain | Residue | Details |
A | HIS627 | |
B | HIS627 |
site_id | SWS_FT_FI3 |
Number of Residues | 8 |
Details | MOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P16332 |
Chain | Residue | Details |
A | LYS89 | |
A | LYS212 | |
A | LYS335 | |
A | LYS602 | |
B | LYS89 | |
B | LYS212 | |
B | LYS335 | |
B | LYS602 |
site_id | SWS_FT_FI4 |
Number of Residues | 4 |
Details | MOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:P16332 |
Chain | Residue | Details |
A | LYS343 | |
A | LYS595 | |
B | LYS343 | |
B | LYS595 |
site_id | SWS_FT_FI5 |
Number of Residues | 2 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:24275569 |
Chain | Residue | Details |
A | SER481 | |
B | SER481 |