Research workbench
Crystallographic structure of sura first peptidyl-prolyl isomerase domain complexed with peptide weyipnv
Analyse Crystallographic structure of sura first peptidyl-prolyl isomerase domain… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2PV1
- Type
- protein
- Length
- 110 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Chaperone sura; Glycosyl transferase, group 1
- EC
- 5.2.1.8
- UniProt
- P0ABZ6, Q2RHX9
Structure
x-ray diffraction · 2 distinct chains · 35% helix, 28% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Chaperone sura (EC 5.2.1.8) | protein | 103 | 38% helix, 30% strand | P0ABZ6 |
| B | Glycosyl transferase, group 1 | protein | 7 | 0% helix, 0% strand | Q2RHX9 |
Interfaces
1 interface between chains.
- A–B · 568 Ų buried · 8 hydrogen bonds · protein-protein
Compared structures
- 2PV1 · Crystallographic Structure of SurA first peptidyl-prolyl isomerase domain complexed with… · the same entry in another collection · chain A against A, TM-score 1.00
- P0ABZ6 · AlphaFold monomer V2.0 prediction for chaperone sura (P0ABZ6) · a predicted model of the same protein · chain A against A, TM-score 0.98
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
- Every structure of UniProt Q2RHX9
- Elsewhere: RCSB PDB 2PV1 · PDBe 2PV1 · UniProt P0ABZ6 · UniProt Q2RHX9
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