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Structure of hisf-D130V+D176V with bound rcdrp

Analyse Structure of hisf-D130V+D176V with bound rcdrp in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4EWN
Type: protein
Length: 243 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Imidazole glycerol phosphate synthase subunit hisf
EC: 4.1.3.-
UniProt: Q9X0C6
Ligands: 0VR
Pockets: 2 · best druggability 0.67

Structure

x-ray diffraction · 1 distinct chain · 39% helix, 25% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
D	Imidazole glycerol phosphate synthase subunit hisf (EC 4.1.3.-)	protein	243	39% helix, 25% strand	Q9X0C6

Ligands and binding sites

0VR · 1-(O-carboxy-phenylamino)-1-deoxy-D-ribulose-5-phosphate · ligand · chains D

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	390	0.67	0.80	47	0VR
2	59	0.30	0.75	15	empty

Compared structures

4EWN · Structure of HisF-D130V+D176V with bound rCdRP · the same entry in another collection · chain D against D, TM-score 1.00
Q9X0C6 · AlphaFold monomer V2.0 prediction for imidazole glycerol phosphate synthase subunit hisf… · a predicted model of the same protein · chain D against A, TM-score 0.95

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 Q9X0C6
Elsewhere: RCSB PDB 4EWN · PDBe 4EWN · UniProt Q9X0C6

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