2XIJ
Crystal structure of human methylmalonyl-CoA mutase in complex with adenosylcobalamin
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 |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 43 |
Details | BINDING SITE FOR RESIDUE B12 A 800 |
Chain | Residue |
A | PHE138 |
A | GLU392 |
A | ALA393 |
A | LEU394 |
A | GLY395 |
A | GLN476 |
A | GLY626 |
A | HIS627 |
A | ASP628 |
A | ARG629 |
A | GLY630 |
A | LEU140 |
A | ILE634 |
A | GLY670 |
A | SER672 |
A | LEU674 |
A | ALA675 |
A | ALA676 |
A | GLY702 |
A | GLY703 |
A | VAL704 |
A | PHE722 |
A | HIS143 |
A | GLY723 |
A | PRO724 |
A | THR726 |
A | 5AD1746 |
A | HOH2253 |
A | HOH2447 |
A | HOH2488 |
A | HOH2508 |
A | HOH3001 |
A | HOH3002 |
A | ALA160 |
A | HOH3003 |
A | HOH3004 |
A | HOH3005 |
A | HOH3006 |
A | VAL227 |
A | ARG228 |
A | THR230 |
A | GLU268 |
A | TRP356 |
site_id | AC2 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE 5AD A 1746 |
Chain | Residue |
A | ALA160 |
A | GLN352 |
A | LEU396 |
A | HOH2173 |
A | HOH2198 |
A | HOH2252 |
A | HOH2507 |
A | HOH2508 |
A | HOH2510 |
A | B12800 |
site_id | AC3 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE SO4 A 1747 |
Chain | Residue |
A | ARG613 |
A | ARG613 |
A | ARG614 |
A | ARG614 |
A | ARG616 |
A | ARG616 |
A | HOH2511 |
A | HOH2511 |
site_id | AC4 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE SO4 A 1748 |
Chain | Residue |
A | TYR146 |
A | ASN150 |
A | ARG152 |
A | HOH2512 |
site_id | AC5 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE EDO A 1749 |
Chain | Residue |
A | SER594 |
A | LYS595 |
A | GLU596 |
A | HOH2513 |
site_id | AC6 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE EDO A 1750 |
Chain | Residue |
A | GLU65 |
A | ASP272 |
A | ILE274 |
A | HOH2035 |
A | HOH2514 |
A | HOH2515 |
site_id | AC7 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE EDO A 1751 |
Chain | Residue |
A | ASP58 |
A | ILE60 |
A | TRP61 |
A | LYS420 |
A | HOH2030 |
A | HOH2516 |
site_id | AC8 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE EDO A 1752 |
Chain | Residue |
A | ARG108 |
A | SER306 |
A | HIS350 |
A | SER384 |
site_id | AC9 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE EDO A 1757 |
Chain | Residue |
A | THR249 |
A | ALA250 |
A | SER258 |
A | ARG304 |
A | HOH2190 |
A | HOH2193 |
site_id | BC1 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE EDO A 1753 |
Chain | Residue |
A | GLU117 |
A | VAL510 |
A | GLN514 |
A | LYS517 |
A | HOH2517 |
site_id | BC2 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE EDO A 1754 |
Chain | Residue |
A | THR216 |
A | GLN218 |
A | SER260 |
A | PHE308 |
A | TYR110 |
A | SER185 |
A | MET186 |
site_id | BC3 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE EDO A 1755 |
Chain | Residue |
A | PRO695 |
A | ILE697 |
A | HOH2485 |
site_id | BC4 |
Number of Residues | 11 |
Details | BINDING SITE FOR RESIDUE BTB A 1756 |
Chain | Residue |
A | ILE107 |
A | ARG108 |
A | GLN109 |
A | TYR110 |
A | ALA111 |
A | GLN131 |
A | SER135 |
A | ARG406 |
A | HOH2079 |
A | HOH2520 |
A | HOH2521 |
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 | 8 |
Details | BINDING: BINDING => ECO:0000269|PubMed:20876572 |
Chain | Residue | Details |
A | GLN50 | |
A | TYR96 | |
A | THR106 | |
A | THR216 | |
A | ARG228 | |
A | LYS255 | |
A | HIS265 | |
A | ARG304 |
site_id | SWS_FT_FI2 |
Number of Residues | 1 |
Details | BINDING: axial binding residue => ECO:0000269|PubMed:20876572 |
Chain | Residue | Details |
A | HIS627 |
site_id | SWS_FT_FI3 |
Number of Residues | 4 |
Details | MOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P16332 |
Chain | Residue | Details |
A | LYS89 | |
A | LYS212 | |
A | LYS335 | |
A | LYS602 |
site_id | SWS_FT_FI4 |
Number of Residues | 2 |
Details | MOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:P16332 |
Chain | Residue | Details |
A | LYS343 | |
A | LYS595 |
site_id | SWS_FT_FI5 |
Number of Residues | 1 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:24275569 |
Chain | Residue | Details |
A | SER481 |