Research workbench
Protein Z in complex with an in vitro selected affibody
Analyse Protein Z in complex with an in vitro selected affibody in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1LP1
- Type
- protein
- Length
- 109 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Affibody binding protein Z; Immunoglobulin G binding protein a
- UniProt
- P38507
- Ligands
- MG, SO4
Structure
x-ray diffraction · 2 distinct chains · 74% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Affibody binding protein Z | protein | 55 | 78% helix, 0% strand | — |
| B | Immunoglobulin G binding protein a | protein | 54 | 70% helix, 0% strand | P38507 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
1 interface between chains.
- A–B · 895 Ų buried · 14 hydrogen bonds · protein-protein
Compared structures
- 1LP1 · Protein Z in complex with an in vitro selected affibody · the same entry in another collection · chain B against B, TM-score 1.00
- P38507 · AlphaFold monomer V2.0 prediction for immunoglobulin G-binding protein a (P38507) · a predicted model of the same protein · chain B against A, TM-score 0.89
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 P38507
- Elsewhere: RCSB PDB 1LP1 · PDBe 1LP1 · UniProt P38507
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