Research workbench
Crystal structure of human methylmalonyl-CoA mutase
Analyse Crystal structure of human methylmalonyl-CoA mutase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3BIC
- Type
- protein
- Length
- 1,430 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Methylmalonyl-CoA mutase, mitochondrial precursor
- EC
- 5.4.99.2
- UniProt
- P22033
- Ligands
- CL
- Pockets
- 11 · best druggability 0.87
Structure
x-ray diffraction · 2 distinct chains · 53% helix, 10% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Methylmalonyl-CoA mutase, mitochondrial precursor (EC 5.4.99.2) | protein | 715 | 53% helix, 10% strand | P22033 |
| B | Methylmalonyl-CoA mutase, mitochondrial precursor (EC 5.4.99.2) | protein | 715 | 53% helix, 10% strand | P22033 |
Ligands and binding sites
- CL · Chloride ion · ion · 4 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
11 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1123 | 0.87 | 0.89 | 123 | CL |
| 2 | 678 | 0.85 | 0.89 | 78 | CL |
| 3 | 388 | 0.77 | 0.86 | 56 | CL |
| 4 | 229 | 0.64 | 0.82 | 42 | empty |
| 5 | 172 | 0.60 | 0.83 | 38 | empty |
Interfaces
1 interface between chains.
- A–B · 3436 Ų buried · 57 hydrogen bonds · protein-protein
Compared structures
- 3BIC · Crystal structure of human methylmalonyl-CoA mutase · the same entry in another collection · chain A against A, TM-score 1.00
- P22033 · AlphaFold monomer V2.0 prediction for methylmalonyl-CoA mutase, mitochondrial (P22033) · a predicted model of the same protein · chain A against A, TM-score 0.98
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt P22033
- Elsewhere: RCSB PDB 3BIC · PDBe 3BIC · UniProt P22033
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