Research workbench
Crystal structure of the holo retinal-bound domain-swapped dimer Q108K:K40L:T51F mutant of human cellular retinol binding protein II
Analyse Crystal structure of the holo retinal-bound domain-swapped dimer… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6MLB
- Type
- protein
- Length
- 532 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P50120
- Ligands
- RET
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D | — | protein | 133 | — | P50120 |
Ligands and binding sites
- RET · Retinal · ligand · 2 copies · chains A, C, B, D
- ACT · Acetate ion · additive · 5 copies · chains A, C, D
- GOL · Glycerol · additive · 4 copies · chains B, D, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6MLB · Crystal structure of the holo retinal-bound domain-swapped dimer Q108K:K40L:T51F mutant… · the same entry in another collection · chain A against A, TM-score 1.00
- P50120 · AlphaFold monomer V2.0 prediction for retinol-binding protein 2 (P50120) · a predicted model of the same protein · chain A against A, TM-score 0.58
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 P50120
- Elsewhere: RCSB PDB 6MLB · PDBe 6MLB · UniProt P50120
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