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Crystal structure of staphylococcus epidermidis aap G58-spacer-G513 (variant G5-spacer-consensus G5)

Analyse Crystal structure of staphylococcus epidermidis aap G58-spacer-G513 (variant… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5TU9
Type: protein
Length: 276 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Accumulation associated protein aap G58-spacer-G513 (variant G5-spacer-consensus G5)
UniProt: Q5HKE8
Pockets: 2 · best druggability 0.47

Structure

x-ray diffraction · 2 distinct chains · 0% helix, 53% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Accumulation associated protein aap G58-spacer-G513 (variant G5-spacer-consensus G5)	protein	139	0% helix, 55% strand	Q5HKE8
B	Accumulation associated protein aap G58-spacer-G513 (variant G5-spacer-consensus G5)	protein	137	0% helix, 51% strand	Q5HKE8

Pockets

2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	118	0.47	0.79	20	empty
2	58	0.29	0.74	16	empty

Interfaces

1 interface between chains.

A–B · 834 Å² buried · 11 hydrogen bonds · protein-protein

Compared structures

5TU9 · Crystal structure of Staphylococcus epidermidis Aap G58-spacer-G513 (variant… · the same entry in another collection · chain A against A, TM-score 1.00

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Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt Q5HKE8
Elsewhere: RCSB PDB 5TU9 · PDBe 5TU9 · UniProt Q5HKE8

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