Research workbench
Crystal structure of a PROM2 containing triple-helical collagen peptide.
Analyse Crystal structure of a PROM2 containing triple-helical collagen peptide. in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6SYJ
- Type
- protein
- Length
- 88 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Ligands
- 2L6, ACE
Structure
x-ray diffraction · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 30 | — | — |
| B, C | — | protein | 29 | — | — |
Ligands and binding sites
- 2L6 · (3s,6r,8as)-5-oxo-1,2,3,8A-tetrahydrospiro[indolizine-6,2'-pyrrolidine]-3-carboxylic acid · ligand · 3 copies · chains A, B, C
- ACE · Acetyl group · ligand · 2 copies · chains B, C, A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6SYJ · Crystal structure of a ProM2 containing triple-helical collagen peptide. · 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 6SYJ · PDBe 6SYJ
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