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Crystal structure of human GDP-D-mannose 4,6-dehydratase (E157Q) in complex with GDP-man
Analyse Crystal structure of human GDP-D-mannose 4,6-dehydratase (E157Q) in complex… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6GPK
- Type
- protein
- Length
- 1,386 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- O60547
- Ligands
- NAP, GDD
Structure
x-ray diffraction · 3 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | — | protein | 350 | — | O60547 |
| C | — | protein | 342 | — | O60547 |
| D | — | protein | 344 | — | O60547 |
Ligands and binding sites
- NAP · Nadp nicotinamide-adenine-dinucleotide phosphate · ligand · 4 copies · chains A, B, C, D
- GDD · Guanosine-5'-diphosphate-alpha-D-mannose · ligand · 4 copies · chains A, B, C, D
- EDO · 1,2-ethanediol · additive · 28 copies · chains A, D, B, C
- GOL · Glycerol · additive · chains C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6GPK · Crystal structure of human GDP-D-mannose 4,6-dehydratase (E157Q) in complex with GDP-Man · the same entry in another collection · chain A against A, TM-score 1.00
- O60547 · AlphaFold monomer V2.0 prediction for GDP-mannose 4,6 dehydratase (O60547) · a predicted model of the same protein · chain C 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 O60547
- Elsewhere: RCSB PDB 6GPK · PDBe 6GPK · UniProt O60547
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