MolNFT v1 · #65793 · protein
Crystal structure of serine hydroxymethyltransferase from mycobacterium tuberculosis
3H7F · Serine hydroxymethyltransferase 1: “Crystal structure of serine hydroxymethyltransferase from mycobacterium tuberculosis”. X-ray diffraction, 1 ligand (MG), 8 pockets (best druggability 0.74). MolNFT v1 #65793 on GenesisL1: 3D…
- PDB
- 3H7F
- Type
- protein
- Length
- 842 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Serine hydroxymethyltransferase 1
- EC
- 2.1.2.1
- UniProt
- O53441
- Ligands
- MG
- Pockets
- 8 · best druggability 0.74
Structure
x-ray diffraction · 2 distinct chains · 51% helix, 13% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Serine hydroxymethyltransferase 1 (EC 2.1.2.1) | protein | 414 | 51% helix, 13% strand | O53441 |
| B | Serine hydroxymethyltransferase 1 (EC 2.1.2.1) | protein | 428 | 50% helix, 13% strand | O53441 |
Ligands and binding sites
- MG · Magnesium ion · metal · chains B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
8 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 395 | 0.74 | 0.84 | 41 | empty |
| 2 | 130 | 0.69 | 0.90 | 24 | empty |
| 3 | 253 | 0.60 | 0.80 | 33 | empty |
| 4 | 74 | 0.52 | 0.85 | 18 | empty |
| 5 | 72 | 0.51 | 0.84 | 20 | empty |
Interfaces
1 interface between chains.
- A–B · 4747 Ų buried · 61 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 modified (cofactor).
Compared structures
- 3H7F · Crystal structure of serine hydroxymethyltransferase from Mycobacterium tuberculosis · the same entry in another collection · 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 O53441
- Elsewhere: RCSB PDB 3H7F · PDBe 3H7F · UniProt O53441
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