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The crystal structure of cbs domain protein from shewanella oneidensis mr-1.

Analyse The crystal structure of cbs domain protein from shewanella oneidensis mr-1. in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3LHH
Type: protein
Length: 125 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Cbs domain protein
UniProt: Q8EDE1
Ligands: AMP
Pockets: 1 · best druggability 0.38

Structure

x-ray diffraction · 1 distinct chain · 36% helix, 25% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Cbs domain protein	protein	125	36% helix, 25% strand	Q8EDE1

Ligands and binding sites

AMP · Adenosine monophosphate · ligand · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

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	77	0.38	0.77	16	AMP

Modifications

Observed in the structure: 7 modified (engineered).

Compared structures

3LHH · The crystal structure of CBS domain protein from Shewanella oneidensis MR-1. · the same entry in another collection · chain A against A, TM-score 1.00

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 Q8EDE1
Elsewhere: RCSB PDB 3LHH · PDBe 3LHH · UniProt Q8EDE1

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