MolNFT v2 · #163200 · protein
Human SHMT2 in complex with pemetrexed
6QVL: “Human SHMT2 in complex with pemetrexed”. X-ray diffraction at 2.28, 3 ligands (PLP, 4DW, CA). MolNFT v2 #163200 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 6QVL
- Type
- protein
- Length
- 907 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 2.28
- Source
- Homo sapiens
- UniProt
- P34897
- Ligands
- PLP, 4DW, CA
Structure
x-ray diffraction · resolution 2.28 · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 453 | — | P34897 |
| B | — | protein | 454 | — | P34897 |
Ligands and binding sites
- PLP · Pyridoxal-5'-phosphate · ligand · 2 copies · chains A, B
- 4DW · N-{4-[2-(2-amino-4-oxo-4,7-dihydro-3H-pyrrolo[2,3-d]pyrimidin-5-yl)ethyl]benzoyl}-L-glutamic acid · ligand · chains A, B
- CA · Calcium ion · metal · chains A
- GOL · Glycerol · additive · 3 copies · chains A, B
- PEG · Di(hydroxyethyl)ether · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
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 P34897
- Elsewhere: RCSB PDB 6QVL · PDBe 6QVL · UniProt P34897
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