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Cis-biphenyl-2,3-dihydrodiol-2,3-dehydrogenase from pseudomonas sp. LB400

Analyse Cis-biphenyl-2,3-dihydrodiol-2,3-dehydrogenase from pseudomonas sp. LB400 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1BDB
Type: protein
Length: 267 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Cis-biphenyl-2,3-dihydrodiol-2,3-dehydrogenase
UniProt: P47227
Ligands: NAD
Pockets: 1 · best druggability 0.77

Structure

x-ray diffraction · 1 distinct chain · 48% helix, 13% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Cis-biphenyl-2,3-dihydrodiol-2,3-dehydrogenase	protein	267	48% helix, 13% strand	P47227

Ligands and binding sites

NAD · Nicotinamide-adenine-dinucleotide · 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, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	515	0.77	0.84	58	NAD

Compared structures

1BDB · Cis-biphenyl-2,3-dihydrodiol-2,3-dehydrogenase from pseudomonas sp. LB400 · the same entry in another collection · chain A against A, TM-score 1.00
P47227 · AlphaFold monomer V2.0 prediction for cis-2,3-dihydrobiphenyl-2,3-diol dehydrogenase… · a predicted model of the same protein · chain A against A, TM-score 0.99

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 P47227
Elsewhere: RCSB PDB 1BDB · PDBe 1BDB · UniProt P47227

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