MolNFT v1 · #177958 · protein
Structure of a triple-helix region of human collagen type xvii
7F01: “Structure of a triple-helix region of human collagen type xvii”. X-ray diffraction, 3 ligands (ACE, NH2, SO4). MolNFT v1 #177958 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 7F01
- Type
- protein
- Length
- 81 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Collagen type xvii
- Ligands
- ACE, NH2, SO4
Structure
x-ray diffraction · 1 distinct chain · 0% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C | Collagen type xvii | protein | 27 | 0% helix, 0% strand | — |
Ligands and binding sites
- ACE · Acetyl group · ligand · 3 copies · chains A, B, C
- NH2 · Amino group · ion · 3 copies · chains A, B, C
- SO4 · Sulfate ion · ion · chains B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
3 interfaces between chains.
- A–B · 996 Ų buried · 12 hydrogen bonds · protein-protein
- B–C · 943 Ų buried · 12 hydrogen bonds · protein-protein
- A–C · 888 Ų buried · 13 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 15 modified, 3 covalent (hydroxylation, covalent ligand).
Compared structures
- 7F01 · Structure of a triple-helix region of human collagen type XVII · 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
- Elsewhere: RCSB PDB 7F01 · PDBe 7F01
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