Research workbench
Oxidoreductase NMDSBA3 from neisseria meningitidis
Analyse Oxidoreductase NMDSBA3 from neisseria meningitidis in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2ZNM
- Type
- protein
- Length
- 740 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- THIOL:DISULFIDE interchange protein dsba
- UniProt
- Q9K0Z4
- Pockets
- 5 · best druggability 0.77
Structure
x-ray diffraction · 3 distinct chains · 49% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | THIOL:DISULFIDE interchange protein dsba | protein | 185 | 49% helix, 14% strand | Q9K0Z4 |
| C | THIOL:DISULFIDE interchange protein dsba | protein | 186 | 48% helix, 13% strand | Q9K0Z4 |
| D | THIOL:DISULFIDE interchange protein dsba | protein | 184 | 49% helix, 14% strand | Q9K0Z4 |
Pockets
5 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1170 | 0.77 | 0.79 | 137 | empty |
| 2 | 644 | 0.75 | 0.81 | 80 | empty |
| 3 | 505 | 0.69 | 0.79 | 65 | empty |
| 4 | 382 | 0.69 | 0.81 | 57 | empty |
| 5 | 62 | 0.38 | 0.79 | 13 | empty |
Interfaces
4 interfaces between chains.
- A–C · 777 Ų buried · 3 hydrogen bonds · protein-protein
- B–D · 765 Ų buried · 5 hydrogen bonds · protein-protein
- A–B · 761 Ų buried · 7 hydrogen bonds · protein-protein
- C–D · 752 Ų buried · 5 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 16 modified (engineered).
Compared structures
- 2ZNM · Oxidoreductase NmDsbA3 from Neisseria meningitidis · 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 Q9K0Z4
- Elsewhere: RCSB PDB 2ZNM · PDBe 2ZNM · UniProt Q9K0Z4
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