Research workbench
Structure of nhp D11A.F2 Fab in complex with 16055 V2B peptide
Analyse Structure of nhp D11A.F2 Fab in complex with 16055 V2B peptide in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6XLZ
- Type
- protein
- Length
- 454 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- A0A0B5KUY7
- Ligands
- SO4
Structure
x-ray diffraction · 4 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| P | — | protein | 20 | — | A0A0B5KUY7 |
| H | — | protein | 214 | — | — |
| L | — | protein | 214 | — | — |
| A | — | protein | 6 | — | A0A0B5KUY7 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 8 copies · chains H, L
- BU3 · (R,R)-2,3-butanediol · additive · 7 copies · chains H, L
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6XLZ · Structure of NHP D11A.F2 Fab in complex with 16055 V2b peptide · the same entry in another collection · chain P against P, 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 A0A0B5KUY7
- Elsewhere: RCSB PDB 6XLZ · PDBe 6XLZ · UniProt A0A0B5KUY7
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