Research workbench
Crystal structure and functional characterization of the thermophilic prolyl isomerase and chaperone slyd
Analyse Crystal structure and functional characterization of the thermophilic prolyl… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3LUO
- Type
- protein
- Length
- 149 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Peptidyl-prolyl cis-trans isomerase; Suc-ala-leu-pro-phe-pna
- EC
- 5.2.1.8
- UniProt
- Q5SLE7
- Ligands
- NIT, ZN
- Pockets
- 1 · best druggability 0.29
Structure
x-ray diffraction · 2 distinct chains · 15% helix, 43% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Peptidyl-prolyl cis-trans isomerase (EC 5.2.1.8) | protein | 145 | 15% helix, 43% strand | Q5SLE7 |
| B | Suc-ala-leu-pro-phe-pna | protein | 4 | 0% helix, 25% strand | — |
Ligands and binding sites
- NIT · 4-nitroaniline · ligand · chains A, B
- ZN · Zinc ion · metal · 4 copies · chains A
- SIN · Succinic acid · additive · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
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 | 59 | 0.29 | 0.74 | 13 | empty |
Interfaces
1 interface between chains.
- A–B · 267 Ų buried · 3 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 covalent (additive adduct, covalent ligand).
Compared structures
- 3LUO · Crystal Structure and functional characterization of the thermophilic prolyl isomerase… · the same entry in another collection · chain A against A, 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 Q5SLE7
- Elsewhere: RCSB PDB 3LUO · PDBe 3LUO · UniProt Q5SLE7
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