Research workbench
Crystal structure of the PEPTIDE(PRO-pro-GLY)3 bound complex of N- terminal domain and peptide substrate binding domain of prolyl-4 hydroxylase (residues 1-238) type I from human
Analyse Crystal structure of the PEPTIDE(PRO-pro-GLY)3 bound complex of N- terminal… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4BT9
- Type
- protein
- Length
- 483 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Prolyl 4-hydroxylase subunit alpha-1; (pro-pro-GLY)3 peptide
- EC
- 1.14.11.2
- UniProt
- P13674
- Pockets
- 4 · best druggability 0.56
Structure
x-ray diffraction · 3 distinct chains · 76% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Prolyl 4-hydroxylase subunit alpha-1 (EC 1.14.11.2) | protein | 236 | 78% helix, 0% strand | P13674 |
| B | Prolyl 4-hydroxylase subunit alpha-1 (EC 1.14.11.2) | protein | 238 | 78% helix, 0% strand | P13674 |
| C | (pro-pro-GLY)3 peptide | protein | 9 | 0% helix, 0% strand | — |
Pockets
4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 225 | 0.56 | 0.78 | 31 | empty |
| 2 | 182 | 0.50 | 0.77 | 27 | empty |
| 3 | 64 | 0.43 | 0.82 | 18 | empty |
| 4 | 66 | 0.32 | 0.75 | 15 | empty |
Interfaces
2 interfaces between chains.
- A–B · 4125 Ų buried · 41 hydrogen bonds · protein-protein
- A–C · 460 Ų buried · 2 hydrogen bonds · protein-protein
Compared structures
- 4BT9 · Crystal structure of the PEPTIDE(PRO-pro-GLY)3 bound complex of N- terminal domain and… · the same entry in another collection · chain A against A, TM-score 1.00
- P13674 · AlphaFold monomer V2.0 prediction for prolyl 4-hydroxylase subunit alpha-1 (P13674) · a predicted model of the same protein · chain A against A, TM-score 0.92
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 P13674
- Elsewhere: RCSB PDB 4BT9 · PDBe 4BT9 · UniProt P13674
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.