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Solution structure of the R2AB repeat domain from staph. epidermidis autolysin (atle)

Analyse Solution structure of the R2AB repeat domain from staph. epidermidis autolysin… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7KWI
Type: protein
Length: 152 residues
Chains: 1
Method: solution nmr
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Bifunctional autolysin
EC: 3.5.1.28, 3.2.1.96
UniProt: O33635
Pockets: 1 · best druggability 0.29

Structure

solution nmr · 1 distinct chain · 2% helix, 46% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Bifunctional autolysin (EC 3.5.1.28, 3.2.1.96)	protein	152	2% helix, 46% strand	O33635

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	71	0.29	0.73	21	empty

Compared structures

7KWI · Solution Structure of the R2ab Repeat Domain from Staph. epidermidis Autolysin (AtlE) · the same entry in another collection · chain A against A, TM-score 1.00
O33635 · AlphaFold monomer V2.0 prediction for bifunctional autolysin (O33635) · 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 O33635
Elsewhere: RCSB PDB 7KWI · PDBe 7KWI · UniProt O33635

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