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Structural basis for allosteric substrate specificity regulation in class III ribonucleotide reductases, native nrdd

Analyse Structural basis for allosteric substrate specificity regulation in class III… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1H7B
Type: protein
Length: 534 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Anaerobic ribonucleotide-triphosphate reductase large chain
EC: 1.17.4.2
UniProt: Q9T0V5
Ligands: PO4
Pockets: 5 · best druggability 0.70

Structure

x-ray diffraction · 1 distinct chain · 45% helix, 15% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Anaerobic ribonucleotide-triphosphate reductase large chain (EC 1.17.4.2)	protein	534	45% helix, 15% strand	Q9T0V5

Ligands and binding sites

PO4 · Phosphate ion · ion · chains A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	628	0.70	0.78	66	PO4
2	178	0.64	0.84	30	empty
3	72	0.39	0.78	12	empty
4	83	0.33	0.74	23	empty
5	74	0.32	0.75	22	empty

Compared structures

1H7B · Structural basis for allosteric substrate specificity regulation in class III… · 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 Q9T0V5
Elsewhere: RCSB PDB 1H7B · PDBe 1H7B · UniProt Q9T0V5

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