Research workbench
Structure of FAB4 bound to P22 TERL(1-33)
Analyse Structure of FAB4 bound to P22 TERL(1-33) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6XMI
- Type
- protein
- Length
- 954 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P26745
Structure
x-ray diffraction · 5 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, D | — | protein | 214 | — | — |
| B | — | protein | 231 | — | — |
| E | — | protein | 232 | — | — |
| F | — | protein | 33 | — | P26745 |
| C | — | protein | 30 | — | P26745 |
Compared structures
- 6XMI · Structure of Fab4 bound to P22 TerL(1-33) · 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
- Every structure of UniProt P26745
- Elsewhere: RCSB PDB 6XMI · PDBe 6XMI · UniProt P26745
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