MolNFT v1 · #12929 · protein

Crystal structure of 2,3-dihydroxybiphenyal dioxygenase (bphc) at 1.45 a resolution

1KW3 · 2,3-dihydroxybiphenyl dioxygenase: “Crystal structure of 2,3-dihydroxybiphenyal dioxygenase (bphc) at 1.45 a resolution”. X-ray diffraction, 1 ligand (FE2), 1 pocket (best druggability 0.59). MolNFT v1 #12929 on GenesisL1: 3D…

PDB: 1KW3
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: FE2
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

FE2 · Fe (II) ion · metal · chains B
MPD · (4S)-2-methyl-2,4-pentanediol · additive · 2 copies · 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	229	0.59	0.80	35	empty

Compared structures

1KW3 · Crystal structure of 2,3-dihydroxybiphenyal dioxygenase (BphC) at 1.45 A resolution · 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

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 P17297
Elsewhere: RCSB PDB 1KW3 · PDBe 1KW3 · UniProt P17297

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