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Crystal structure of anthranilate synthase component I from streptococcus pneumoniae TIGR4

Analyse Crystal structure of anthranilate synthase component I from streptococcus… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5KCK
Type: protein
Length: 435 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Anthranilate synthase component I
EC: 4.1.3.27
UniProt: A0A0H2URN1
Pockets: 4 · best druggability 0.72

Structure

x-ray diffraction · 1 distinct chain · 30% helix, 29% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Anthranilate synthase component I (EC 4.1.3.27)	protein	435	30% helix, 29% strand	A0A0H2URN1

Ligands and binding sites

GOL · Glycerol · additive · 2 copies · chains A

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

Pockets

4 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	673	0.72	0.79	58	empty
2	67	0.71	0.96	18	empty
3	701	0.69	0.76	52	empty
4	71	0.53	0.86	20	empty

Modifications

Observed in the structure: 14 modified (engineered).

Compared structures

5KCK · Crystal structure of anthranilate synthase component I from Streptococcus pneumoniae TIGR4 · 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 A0A0H2URN1
Elsewhere: RCSB PDB 5KCK · PDBe 5KCK · UniProt A0A0H2URN1

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