MolNFT v1 · #153636 · protein
Structure of a triple-helix region of human collagen type II
6JKL: “Structure of a triple-helix region of human collagen type II”. X-ray diffraction, 2 ligands (ACE, NH2). MolNFT v1 #153636 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 6JKL
- Type
- protein
- Length
- 81 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- A triple-helix region of human collagen type II
- Ligands
- ACE, NH2
Structure
x-ray diffraction · 1 distinct chain · 0% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C | A triple-helix region of human collagen type II | protein | 27 | 0% helix, 0% strand | — |
Ligands and binding sites
- ACE · Acetyl group · ligand · 2 copies · chains A, B, C
- NH2 · Amino group · ion · 2 copies · chains A, B, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
3 interfaces between chains.
- A–C · 847 Ų buried · 9 hydrogen bonds · protein-protein
- B–C · 828 Ų buried · 9 hydrogen bonds · protein-protein
- A–B · 800 Ų buried · 8 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 18 modified, 2 covalent (hydroxylation, covalent ligand).
Compared structures
- 6JKL · Structure of a triple-helix region of human collagen type II · the same entry in another collection · chain B against B, 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 6JKL · PDBe 6JKL
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