MolNFT v1 · #87836 · protein
Crystal structure of human 5-methyltetrahydrofolate-homocysteine methyltransferase, the homocysteine and folate binding domains
4CCZ · Methionine synthase: “Crystal structure of human 5-methyltetrahydrofolate-homocysteine methyltransferase, the homocysteine and…”. X-ray diffraction, 1 ligand (THG), 8 pockets (best druggability 0.65). MolNFT v1 #87836 on GenesisL1…
- PDB
- 4CCZ
- Type
- protein
- Length
- 611 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Methionine synthase
- EC
- 2.1.1.13
- UniProt
- Q99707
- Ligands
- THG
- Pockets
- 8 · best druggability 0.65
Structure
x-ray diffraction · 1 distinct chain · 47% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Methionine synthase (EC 2.1.1.13) | protein | 611 | 47% helix, 15% strand | Q99707 |
Ligands and binding sites
- THG · (6S)-5,6,7,8-tetrahydrofolate · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
8 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 52 | 0.65 | 0.95 | 19 | empty |
| 2 | 283 | 0.64 | 0.81 | 42 | empty |
| 3 | 380 | 0.64 | 0.78 | 43 | empty |
| 4 | 57 | 0.64 | 0.93 | 20 | empty |
| 5 | 374 | 0.60 | 0.77 | 46 | THG |
Modifications
Observed in the structure: 1 disulfide (disulfide).
Compared structures
- 4CCZ · Crystal structure of human 5-methyltetrahydrofolate-homocysteine methyltransferase, the… · the same entry in another collection · chain A against A, TM-score 1.00
- Q99707 · AlphaFold monomer V2.0 prediction for methionine synthase (Q99707) · a predicted model of the same protein · chain A against A, TM-score 1.00
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 Q99707
- Elsewhere: RCSB PDB 4CCZ · PDBe 4CCZ · UniProt Q99707
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