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Crystal structure of a staphylococcal INHIBITOR/CHAPERONE

Analyse Crystal structure of a staphylococcal INHIBITOR/CHAPERONE in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1QWX
Type: protein
Length: 216 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Cysteine protease
UniProt: Q7A189

Structure

x-ray diffraction · 1 distinct chain · 10% helix, 56% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Cysteine protease	protein	108	10% helix, 56% strand	Q7A189

Interfaces

1 interface between chains.

A–B · 642 Å² buried · 6 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 6 modified (engineered).

Compared structures

1QWX · Crystal Structure of a Staphylococcal Inhibitor/Chaperone · the same entry in another collection · chain A against A, TM-score 1.00
Q7A189 · AlphaFold monomer V2.0 prediction for staphostatin B (Q7A189) · a predicted model of the same protein · chain A against A, TM-score 0.95

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 Q7A189
Elsewhere: RCSB PDB 1QWX · PDBe 1QWX · UniProt Q7A189

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