MolNFT v1 · #114193 · protein
Crystal structure of heme binding protein hmut Y240A
5B50 · ABC-type transporter, periplasmic component: “Crystal structure of heme binding protein hmut Y240A”. X-ray diffraction, 1 ligand (HEM), 2 pockets (best druggability 0.55). MolNFT v1 #114193 on GenesisL1: 3D structure, binding sites…
- PDB
- 5B50
- Type
- protein
- Length
- 324 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- ABC-type transporter, periplasmic component
- UniProt
- Q8NTB8
- Ligands
- HEM
- Pockets
- 2 · best druggability 0.55
Structure
x-ray diffraction · 1 distinct chain · 42% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | ABC-type transporter, periplasmic component | protein | 324 | 42% helix, 17% strand | Q8NTB8 |
Ligands and binding sites
- HEM · Protoporphyrin IX containing Fe · ligand · 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, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 179 | 0.55 | 0.79 | 22 | HEM |
| 2 | 94 | 0.38 | 0.76 | 19 | empty |
Compared structures
- 5B50 · Crystal structure of heme binding protein HmuT Y240A · 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 Q8NTB8
- Elsewhere: RCSB PDB 5B50 · PDBe 5B50 · UniProt Q8NTB8
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