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Crystal structure of bphc-2,3-dihydroxybiphenyl-no complex

Analyse Crystal structure of bphc-2,3-dihydroxybiphenyl-no complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1KW8
Type: protein
Length: 288 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: 2,3-dihydroxybiphenyl dioxygenase
EC: 1.13.11.39
UniProt: P17297
Ligands: BPY, FE2, NO
Pockets: 1 · best druggability 0.59

Structure

x-ray diffraction · 1 distinct chain · 20% helix, 39% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
B	2,3-dihydroxybiphenyl dioxygenase (EC 1.13.11.39)	protein	288	20% helix, 39% strand	P17297

Ligands and binding sites

BPY · Biphenyl-2,3-diol · ligand · chains B
FE2 · Fe (II) ion · metal · chains B
NO · Nitric oxide · ion · chains B

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	199	0.59	0.81	32	FE2, NO, BPY

Compared structures

1KW8 · Crystal structure of BphC-2,3-dihydroxybiphenyl-NO complex · the same entry in another collection · chain B against B, TM-score 1.00
P17297 · AlphaFold monomer V2.0 prediction for biphenyl-2,3-diol 1,2-dioxygenase (P17297) · a predicted model of the same protein · chain B 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 P17297
Elsewhere: RCSB PDB 1KW8 · PDBe 1KW8 · UniProt P17297

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