Research workbench
Crystal structure of wild type peptide-binding domain of human type I collagen prolyl 4-hydroxylase.
Analyse Crystal structure of wild type peptide-binding domain of human type I collagen… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2V5F
- Type
- protein
- Length
- 103 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P13674
Structure
x-ray diffraction · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 97 | — | P13674 |
| X | — | protein | 6 | — | — |
Compared structures
- 2V5F · Crystal structure of wild type peptide-binding domain of human type I collagen prolyl… · 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 0.99
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 2V5F · PDBe 2V5F · UniProt P13674
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