Research workbench
NMR structure of the E. COLI peptidyl-prolyl CIS/TRANS-isomerase parvulin 10
Analyse NMR structure of the E. COLI peptidyl-prolyl CIS/TRANS-isomerase parvulin 10 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1JNS
- Type
- protein
- Length
- 92 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Peptidyl-prolyl cis-trans isomerase C
- EC
- 5.2.1.8
- UniProt
- P0A9L5
- Pockets
- 1 · best druggability 0.39
Structure
solution nmr · 1 distinct chain · 37% helix, 28% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Peptidyl-prolyl cis-trans isomerase C (EC 5.2.1.8) | protein | 92 | 37% helix, 28% strand | P0A9L5 |
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 84 | 0.39 | 0.77 | 13 | empty |
Compared structures
- 1JNS · NMR Structure of the E. coli Peptidyl-Prolyl cis/trans-Isomerase Parvulin 10 · the same entry in another collection · chain A against A, TM-score 1.00
- P0A9L5 · AlphaFold monomer V2.0 prediction for peptidyl-prolyl cis-trans isomerase C (P0A9L5) · a predicted model of the same protein · chain A against A, TM-score 0.82
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 P0A9L5
- Elsewhere: RCSB PDB 1JNS · PDBe 1JNS · UniProt P0A9L5
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