Research workbench
Structure of the haem-chaperone proteobacteria-protein hems
Analyse Structure of the haem-chaperone proteobacteria-protein hems in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2J0P
- Type
- protein
- Length
- 328 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Hemin transport protein hems
- UniProt
- P31517
- Ligands
- HEM
- Pockets
- 2 · best druggability 0.71
Structure
x-ray diffraction · 1 distinct chain · 30% helix, 34% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Hemin transport protein hems | protein | 328 | 30% helix, 34% strand | P31517 |
Ligands and binding sites
- HEM · Protoporphyrin IX containing Fe · ligand · chains A
- 12P · Dodecaethylene glycol · additive · chains A
- MLI · Malonate ion · additive · chains A
- PEG · Di(hydroxyethyl)ether · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 638 | 0.71 | 0.78 | 60 | HEM |
| 2 | 379 | 0.67 | 0.80 | 36 | PEG |
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 P31517
- Elsewhere: RCSB PDB 2J0P · PDBe 2J0P · UniProt P31517
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