Research workbench
The crystal structure of transferrin binding protein a (tbpa) from neisseria meningitidis serogroup B in complex with the C-lobe of human transferrin
Analyse The crystal structure of transferrin binding protein a (tbpa) from neisseria… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3V89
- Type
- protein
- Length
- 1,192 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Transferrin-binding protein a; Serotransferrin
- UniProt
- Q9JPJ0, P02787
- Pockets
- 16 · best druggability 0.88
Structure
x-ray diffraction · 2 distinct chains · 14% helix, 40% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Transferrin-binding protein a | protein | 853 | 7% helix, 49% strand | Q9JPJ0 |
| B | Serotransferrin | protein | 339 | 33% helix, 17% strand | P02787 |
Pockets
16 pockets found on a 1 Å grid, 8 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 627 | 0.88 | 0.93 | 81 | empty |
| 2 | 1079 | 0.82 | 0.83 | 111 | empty |
| 3 | 264 | 0.75 | 0.88 | 40 | empty |
| 4 | 602 | 0.74 | 0.81 | 90 | empty |
| 5 | 634 | 0.69 | 0.77 | 70 | empty |
Interfaces
1 interface between chains.
- A–B · 2375 Ų buried · 30 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 14 disulfide (disulfide).
Compared structures
- 3V89 · The crystal structure of transferrin binding protein A (TbpA) from Neisseria meningitidis… · the same entry in another collection · chain B against B, TM-score 1.00
- P02787 · AlphaFold monomer V2.0 prediction for serotransferrin (P02787) · a predicted model of the same protein · chain B against A, TM-score 0.87
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 Q9JPJ0
- Every structure of UniProt P02787
- Elsewhere: RCSB PDB 3V89 · PDBe 3V89 · UniProt Q9JPJ0 · UniProt P02787
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