Research workbench
The crystal structure of neisseria gonorrhoeae dolp (NGO1985)
Analyse The crystal structure of neisseria gonorrhoeae dolp (NGO1985) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6XMV
- Type
- protein
- Length
- 307 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- HEMOLYSIN,ENDOLYSIN
- EC
- 3.2.1.17
- UniProt
- Q5F5E4, D9IEF7
- Ligands
- CL
- Pockets
- 2 · best druggability 0.68
Structure
x-ray diffraction · 1 distinct chain · 52% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | HEMOLYSIN,ENDOLYSIN (EC 3.2.1.17) | protein | 307 | 52% helix, 20% strand | Q5F5E4, D9IEF7 |
Ligands and binding sites
- CL · Chloride ion · ion · 2 copies · 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 | 448 | 0.68 | 0.80 | 50 | empty |
| 2 | 73 | 0.30 | 0.74 | 14 | empty |
Compared structures
- 6XMV · The crystal structure of Neisseria gonorrhoeae DolP (NGO1985) · 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 Q5F5E4
- Every structure of UniProt D9IEF7
- Elsewhere: RCSB PDB 6XMV · PDBe 6XMV · UniProt Q5F5E4 · UniProt D9IEF7
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