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Crystal structure of kred mutant-F147L/L153Q/Y190P/L199A/M205F/M206F
Analyse Crystal structure of kred mutant-F147L/L153Q/Y190P/L199A/M205F/M206F in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7VE7
- Type
- protein
- Length
- 1,005 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q6WVP7
- Ligands
- NAP, MG
Structure
x-ray diffraction · 3 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 253 | — | Q6WVP7 |
| B | — | protein | 250 | — | Q6WVP7 |
| C, D | — | protein | 251 | — | Q6WVP7 |
Ligands and binding sites
- NAP · Nadp nicotinamide-adenine-dinucleotide phosphate · ligand · 4 copies · chains A, B, C, D
- MG · Magnesium ion · metal · 2 copies · chains A, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 7VE7 · Crystal structure of KRED mutant-F147L/L153Q/Y190P/L199A/M205F/M206F · 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 Q6WVP7
- Elsewhere: RCSB PDB 7VE7 · PDBe 7VE7 · UniProt Q6WVP7
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