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Crystal structure of para-aminobenzoate synthetase, component I from cytophaga hutchinsonii

Analyse Crystal structure of para-aminobenzoate synthetase, component I from cytophaga… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3H9M
Type: protein
Length: 399 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: P-aminobenzoate synthetase, component I
EC: 4.1.3.-
UniProt: Q11U39
Pockets: 2 · best druggability 0.67

Structure

x-ray diffraction · 1 distinct chain · 31% helix, 32% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	P-aminobenzoate synthetase, component I (EC 4.1.3.-)	protein	399	31% helix, 32% strand	Q11U39

Ligands and binding sites

DTU · (2R,3S)-1,4-dimercaptobutane-2,3-diol · additive · chains A
PGE · Triethylene glycol · additive · chains A

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

Pockets

2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	357	0.67	0.81	36	empty
2	118	0.41	0.76	29	empty

Modifications

Observed in the structure: 9 modified (engineered).

Compared structures

3H9M · Crystal structure of para-aminobenzoate synthetase, component I from Cytophaga… · 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 Q11U39
Elsewhere: RCSB PDB 3H9M · PDBe 3H9M · UniProt Q11U39

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