Research workbench
Prnb 7-cl-D-tryptophan complex
Analyse Prnb 7-cl-D-tryptophan complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2V7M
- Type
- protein
- Length
- 343 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Prnb
- UniProt
- P95481
- Ligands
- HEM, DTE, PO4
- Pockets
- 1 · best druggability 0.81
Structure
x-ray diffraction · 1 distinct chain · 69% helix, 2% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Prnb | protein | 343 | 69% helix, 2% strand | P95481 |
Ligands and binding sites
- HEM · Protoporphyrin IX containing Fe · ligand · chains A
- DTE · 7-cl-D-tryptophan · ligand · chains A
- PO4 · Phosphate ion · ion · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 554 | 0.81 | 0.86 | 54 | HEM, DTE |
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 P95481
- Elsewhere: RCSB PDB 2V7M · PDBe 2V7M · UniProt P95481
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