Research workbench
A. thaliana serine hydroxymethyltransferase isoform 2 (ATSHMT2) in complex with methotrexate
Analyse A. thaliana serine hydroxymethyltransferase isoform 2 (ATSHMT2) in complex with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6SMN
- Type
- protein
- Length
- 1,913 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q94C74
Structure
x-ray diffraction · 3 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | — | protein | 477 | — | Q94C74 |
| C | — | protein | 478 | — | Q94C74 |
| D | — | protein | 481 | — | Q94C74 |
Ligands and binding sites
- EDO · 1,2-ethanediol · additive · 48 copies · chains A, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6SMN · A. thaliana serine hydroxymethyltransferase isoform 2 (AtSHMT2) in complex with… · the same entry in another collection · chain D against D, TM-score 1.00
- Q94C74 · AlphaFold monomer V2.0 prediction for serine hydroxymethyltransferase 2, mitochondrial… · a predicted model of the same protein · chain D against A, TM-score 0.99
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 Q94C74
- Elsewhere: RCSB PDB 6SMN · PDBe 6SMN · UniProt Q94C74
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