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M. thermoresistible impdh in complex with imp and compound 2 (NMR744)

Analyse M. thermoresistible impdh in complex with imp and compound 2 (NMR744) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5OU2
Type: protein
Length: 330 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Inosine-5'-monophosphate DEHYDROGENASE,INOSINE-5'- monophosphate dehydrogenase
EC: 1.1.1.205
UniProt: G7CNL4
Ligands: 36Y, IMP
Pockets: 1 · best druggability 0.74

Structure

x-ray diffraction · 1 distinct chain · 37% helix, 20% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Inosine-5'-monophosphate DEHYDROGENASE,INOSINE-5'- monophosphate dehydrogenase (EC 1.1.1.205)	protein	330	37% helix, 20% strand	G7CNL4

Ligands and binding sites

36Y · 4-(4-bromophenyl)-1H-imidazole · ligand · 2 copies · chains A
IMP · Inosinic acid · ligand · chains A

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	398	0.74	0.84	41	IMP, 36Y

Compared structures

5OU2 · M. thermoresistible IMPDH in complex with IMP and Compound 2 (NMR744) · 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 G7CNL4
Elsewhere: RCSB PDB 5OU2 · PDBe 5OU2 · UniProt G7CNL4

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