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1.5A crystal structure of the protein PG130 from staphylococcus aureus, structural genomics

Analyse 1.5A crystal structure of the protein PG130 from staphylococcus aureus… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1SQE
Type: protein
Length: 207 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Hypothetical protein PG130
UniProt: Q99X56
Pockets: 2 · best druggability 0.59

Structure

x-ray diffraction · 2 distinct chains · 22% helix, 43% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Hypothetical protein PG130	protein	101	25% helix, 43% strand	Q99X56
B	Hypothetical protein PG130	protein	106	20% helix, 42% strand	Q99X56

Pockets

2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	168	0.59	0.82	21	empty
2	106	0.45	0.78	22	empty

Interfaces

1 interface between chains.

A–B · 1573 Å² buried · 35 hydrogen bonds · protein-protein

Compared structures

1SQE · 1.5A Crystal Structure Of the protein PG130 from Staphylococcus aureus, Structural… · the same entry in another collection · chain A against A, TM-score 1.00
Q99X56 · AlphaFold monomer V2.0 prediction for heme oxygenase (staphylobilin- producing) 2 (Q99X56) · a predicted model of the same protein · chain A against A, TM-score 0.90

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 Q99X56
Elsewhere: RCSB PDB 1SQE · PDBe 1SQE · UniProt Q99X56

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