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Crystal structure of type-III secretion chaperone ipgc from shigella flexneri (residues 10-155)
Analyse Crystal structure of type-III secretion chaperone ipgc from shigella flexneri… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3KS2
- Type
- protein
- Length
- 2,466 residues
- Chains
- 18
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Chaperone protein ipgc
- UniProt
- P0A2U4
- Pockets
- 20 · best druggability 0.60
Structure
x-ray diffraction · 1 distinct chain · 71% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P, Q, R | Chaperone protein ipgc | protein | 137 | 71% helix, 0% strand | P0A2U4 |
Pockets
20 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 418 | 0.60 | 0.76 | 45 | empty |
| 2 | 357 | 0.55 | 0.74 | 52 | empty |
| 3 | 231 | 0.52 | 0.76 | 30 | empty |
| 4 | 176 | 0.47 | 0.76 | 23 | empty |
| 5 | 69 | 0.47 | 0.83 | 21 | empty |
Interfaces
23 interfaces between chains.
- Q–R · 1472 Ų buried · 17 hydrogen bonds · protein-protein
- G–H · 1387 Ų buried · 6 hydrogen bonds · protein-protein
- C–D · 1379 Ų buried · 5 hydrogen bonds · protein-protein
- O–P · 1370 Ų buried · 8 hydrogen bonds · protein-protein
- K–L · 1358 Ų buried · 6 hydrogen bonds · protein-protein
Compared structures
- 3KS2 · Crystal Structure of Type-III Secretion Chaperone IpgC from Shigella flexneri (residues… · the same entry in another collection · chain R against R, 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 P0A2U4
- Elsewhere: RCSB PDB 3KS2 · PDBe 3KS2 · UniProt P0A2U4
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