MolNFT v1 · #158152 · protein
Structure of human triose phosphate isomerase R189A
6NLH: “Structure of human triose phosphate isomerase R189A”. X-ray diffraction, 3 ligands (NA, BR, PO4). MolNFT v1 #158152 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 6NLH
- Type
- protein
- Length
- 1,934 residues
- Chains
- 8
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P60174
- Ligands
- NA, BR, PO4
Structure
x-ray diffraction · 5 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 244 | — | P60174 |
| E | — | protein | 238 | — | P60174 |
| B, D, G | — | protein | 245 | — | P60174 |
| C, F | — | protein | 239 | — | P60174 |
| H | — | protein | 239 | — | P60174 |
Ligands and binding sites
- NA · Sodium ion · metal · 20 copies · chains A, E, B, C, D, F, G, H
- BR · Bromide ion · ion · 4 copies · chains E, C, F, H
- PO4 · Phosphate ion · ion · 4 copies · chains E, C, F, H
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 P60174
- Elsewhere: RCSB PDB 6NLH · PDBe 6NLH · UniProt P60174
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