Research workbench
Crystal structure of the Fab antibody complexed with human ykl-40
Analyse Crystal structure of the Fab antibody complexed with human ykl-40 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7CJ2
- Type
- protein
- Length
- 1,533 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- A0A024R969
- Ligands
- NAG, BMA
Structure
x-ray diffraction · 5 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| C | — | protein | 204 | — | — |
| D | — | protein | 211 | — | — |
| A, B | — | protein | 361 | — | A0A024R969 |
| K | — | protein | 188 | — | — |
| L | — | protein | 208 | — | — |
Ligands and binding sites
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 4 copies · chains C, A, B, K
- BMA · beta-D-mannopyranose · sugar
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 7CJ2 · Crystal structure of the Fab antibody complexed with human YKL-40 · the same entry in another collection · chain C against C, 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
- Every structure of UniProt A0A024R969
- Elsewhere: RCSB PDB 7CJ2 · PDBe 7CJ2 · UniProt A0A024R969
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