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Crystal structure glycohydrolase

Analyse Crystal structure glycohydrolase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3G9D
Type: protein
Length: 580 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Dinitrogenase reductase activacting glicohydrolase
EC: 3.2.2.24
UniProt: A7XNI2
Ligands: MG
Pockets: 4 · best druggability 0.63

Structure

x-ray diffraction · 2 distinct chains · 64% helix, 1% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Dinitrogenase reductase activacting glicohydrolase (EC 3.2.2.24)	protein	290	63% helix, 1% strand	A7XNI2
B	Dinitrogenase reductase activacting glicohydrolase (EC 3.2.2.24)	protein	290	66% helix, 1% strand	A7XNI2

Ligands and binding sites

MG · Magnesium ion · metal · 4 copies · chains A, B

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

Pockets

4 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	338	0.63	0.79	45	MG
2	147	0.49	0.78	23	empty
3	112	0.42	0.77	25	MG
4	65	0.32	0.76	12	empty

Interfaces

1 interface between chains.

A–B · 737 Å² buried · 17 hydrogen bonds · protein-protein

Compared structures

3G9D · Crystal structure glycohydrolase · 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 A7XNI2
Elsewhere: RCSB PDB 3G9D · PDBe 3G9D · UniProt A7XNI2

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