MolNFT v1 · #7101 · protein
Crystal structure of kdpg aldolase double mutant K133Q/T161K
1FWR: “Crystal structure of kdpg aldolase double mutant K133Q/T161K”. X-ray diffraction, 8 pockets (best druggability 0.76). MolNFT v1 #7101 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 1FWR
- Type
- protein
- Length
- 639 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Kdpg aldolase
- EC
- 4.1.2.14
- UniProt
- P0A955
- Pockets
- 8 · best druggability 0.76
Structure
x-ray diffraction · 1 distinct chain · 42% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C | Kdpg aldolase (EC 4.1.2.14) | protein | 213 | 42% helix, 17% strand | P0A955 |
Ligands and binding sites
- CIT · Citric acid · additive · 3 copies · chains A, C, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
8 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 219 | 0.76 | 0.91 | 28 | empty |
| 2 | 124 | 0.69 | 0.90 | 28 | empty |
| 3 | 194 | 0.55 | 0.79 | 41 | CIT |
| 4 | 165 | 0.53 | 0.79 | 25 | CIT |
| 5 | 148 | 0.52 | 0.79 | 26 | CIT |
Interfaces
3 interfaces between chains.
- A–C · 587 Ų buried · 5 hydrogen bonds · protein-protein
- A–B · 573 Ų buried · 2 hydrogen bonds · protein-protein
- B–C · 570 Ų buried · 2 hydrogen bonds · protein-protein
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 P0A955
- Elsewhere: RCSB PDB 1FWR · PDBe 1FWR · UniProt P0A955
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