Research workbench
Plp-bound form of a putative cystathionine gamma-lyase
Analyse Plp-bound form of a putative cystathionine gamma-lyase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6K1N
- Type
- protein
- Length
- 1,493 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- B4SII9
- Ligands
- PLP
Structure
x-ray diffraction · 4 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 370 | — | B4SII9 |
| B | — | protein | 378 | — | B4SII9 |
| C | — | protein | 371 | — | B4SII9 |
| D | — | protein | 374 | — | B4SII9 |
Ligands and binding sites
- PLP · Pyridoxal-5'-phosphate · ligand · 4 copies · chains A, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6K1N · PLP-bound form of a putative cystathionine gamma-lyase · 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 B4SII9
- Elsewhere: RCSB PDB 6K1N · PDBe 6K1N · UniProt B4SII9
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