MolNFT v1 · #30226 · protein
Crystal structure of an atypical cyclophilin (peptidylprolyl cis-trans isomerase) (TM1367) from thermotoga maritima at 1.90 a resolution
1ZX8 · Hypothetical protein TM1367: “Crystal structure of an atypical cyclophilin (peptidylprolyl cis-trans isomerase) (TM1367) from thermotoga…”. X-ray diffraction, 1 ligand (NI), 3 pockets (best druggability 0.72). MolNFT v1 #30226 on…
- PDB
- 1ZX8
- Type
- protein
- Length
- 382 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Hypothetical protein TM1367
- UniProt
- Q9X187
- Ligands
- NI
- Pockets
- 3 · best druggability 0.72
Structure
x-ray diffraction · 2 distinct chains · 14% helix, 42% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Hypothetical protein TM1367 | protein | 127 | 14% helix, 43% strand | Q9X187 |
| C | Hypothetical protein TM1367 | protein | 128 | 14% helix, 42% strand | Q9X187 |
Ligands and binding sites
- NI · Nickel (II) ion · metal · chains C
- 1PE · Pentaethylene glycol · additive · 3 copies · chains A, B, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 73 | 0.72 | 0.95 | 21 | 1PE |
| 2 | 158 | 0.48 | 0.77 | 33 | empty |
| 3 | 224 | 0.48 | 0.74 | 36 | empty |
Interfaces
2 interfaces between chains.
- B–C · 439 Ų buried · 2 hydrogen bonds · protein-protein
- A–B · 54 Ų buried · 0 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 9 modified (engineered).
Compared structures
- 1ZX8 · CRYSTAL STRUCTURE OF an atypical cyclophilin (peptidylprolyl cis-trans 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 Q9X187
- Elsewhere: RCSB PDB 1ZX8 · PDBe 1ZX8 · UniProt Q9X187
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