MolNFT v1 · #171892 · protein
Plant nucleoside hydrolase - ZMNRH3 enzyme in complex with forodesine
6ZK5: “Plant nucleoside hydrolase - ZMNRH3 enzyme in complex with forodesine”. X-ray diffraction, 2 ligands (IMH, CA). MolNFT v1 #171892 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 6ZK5
- Type
- protein
- Length
- 632 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- B6T563
- Ligands
- IMH, CA
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | — | protein | 316 | — | B6T563 |
Ligands and binding sites
- IMH · 1,4-dideoxy-4-aza-1-(S)-(9-deazahypoxanthin-9-yl)-D-ribitol · ligand · 2 copies · chains A, B
- CA · Calcium ion · metal · 2 copies · chains A, B
- EDO · 1,2-ethanediol · additive · 2 copies · chains A, B
- PGE · Triethylene glycol · additive · chains B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6ZK5 · Plant nucleoside hydrolase - ZmNRh3 enzyme in complex with forodesine · 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 B6T563
- Elsewhere: RCSB PDB 6ZK5 · PDBe 6ZK5 · UniProt B6T563
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