MolNFT v1 · #124553 · protein
Cmla beta-hydroxylase in chemically reduced diferrous state
5KIK · Cmla protein: “Cmla beta-hydroxylase in chemically reduced diferrous state”. X-ray diffraction, 2 ligands (FE, K), 6 pockets (best druggability 0.68). MolNFT v1 #124553 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 5KIK
- Type
- protein
- Length
- 521 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cmla protein
- UniProt
- F2RB80
- Ligands
- FE, K
- Pockets
- 6 · best druggability 0.68
Structure
x-ray diffraction · 1 distinct chain · 35% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Cmla protein | protein | 521 | 35% helix, 22% strand | F2RB80 |
Ligands and binding sites
- FE · Fe (III) ion · metal · 2 copies · chains A
- K · Potassium ion · metal · chains A
- GOL · Glycerol · additive · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
6 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 349 | 0.68 | 0.82 | 42 | empty |
| 2 | 75 | 0.61 | 0.90 | 22 | empty |
| 3 | 161 | 0.54 | 0.80 | 25 | empty |
| 4 | 248 | 0.51 | 0.75 | 23 | empty |
| 5 | 89 | 0.46 | 0.80 | 18 | empty |
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 F2RB80
- Elsewhere: RCSB PDB 5KIK · PDBe 5KIK · UniProt F2RB80
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