Research workbench
BMP1 complexed with a reverse hydroxymate - compound 22
Analyse BMP1 complexed with a reverse hydroxymate - compound 22 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6BSL
- Type
- protein
- Length
- 401 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P13497
- Ligands
- ACE, EVV, ZN, SCN
Structure
x-ray diffraction · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 201 | — | P13497 |
| B | — | protein | 200 | — | P13497 |
Ligands and binding sites
- ACE · Acetyl group · ligand · chains A
- EVV · N-(2-ethoxy-4-{5-[({[(2R)-2-{(1R)-1-[formyl(hydroxy) amino]propyl}heptanoyl]amino}methyl)carbamoyl]furan-2-yl}benzene-1-carbonyl)-L-aspartic acid · ligand · chains A, B
- ZN · Zinc ion · metal · 3 copies · chains A, B
- SCN · Thiocyanate ion · ion · 2 copies · chains A, B
- EDO · 1,2-ethanediol · additive · 3 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
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 P13497
- Elsewhere: RCSB PDB 6BSL · PDBe 6BSL · UniProt P13497
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.