Research workbench
Crystallographic structure of sura, a molecular chaperone that facilitates outer membrane porin folding
Analyse Crystallographic structure of sura, a molecular chaperone that facilitates… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1M5Y
- Type
- protein
- Length
- 1,530 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Survival protein sura
- EC
- 5.2.1.8
- UniProt
- P0ABZ6
- Pockets
- 13 · best druggability 0.72
Structure
x-ray diffraction · 4 distinct chains · 51% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Survival protein sura (EC 5.2.1.8) | protein | 388 | 51% helix, 18% strand | P0ABZ6 |
| B | Survival protein sura (EC 5.2.1.8) | protein | 377 | 51% helix, 18% strand | P0ABZ6 |
| C | Survival protein sura (EC 5.2.1.8) | protein | 376 | 51% helix, 18% strand | P0ABZ6 |
| D | Survival protein sura (EC 5.2.1.8) | protein | 389 | 51% helix, 19% strand | P0ABZ6 |
Pockets
13 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 697 | 0.72 | 0.79 | 61 | empty |
| 2 | 666 | 0.72 | 0.79 | 68 | empty |
| 3 | 705 | 0.72 | 0.78 | 64 | empty |
| 4 | 673 | 0.71 | 0.78 | 65 | empty |
| 5 | 237 | 0.51 | 0.75 | 36 | empty |
Compared structures
- 1M5Y · Crystallographic Structure of SurA, a Molecular Chaperone that Facilitates Outer Membrane… · the same entry in another collection · chain D against D, TM-score 1.00
- P0ABZ6 · AlphaFold monomer V2.0 prediction for chaperone sura (P0ABZ6) · a predicted model of the same protein · chain D against A, TM-score 0.90
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 P0ABZ6
- Elsewhere: RCSB PDB 1M5Y · PDBe 1M5Y · UniProt P0ABZ6
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