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Crystal structure of alanine DEHYDROGENASE/PYRIDINE nucleotide transhydrogenase from mycobacterium smegmatis

Analyse Crystal structure of alanine DEHYDROGENASE/PYRIDINE nucleotide transhydrogenase… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3P2Y
Type: protein
Length: 345 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Alanine DEHYDROGENASE/PYRIDINE nucleotide transhydrogenase
EC: 1.4.1.1
UniProt: A0QNT0
Ligands: CA, NA
Pockets: 1 · best druggability 0.72

Structure

x-ray diffraction · 1 distinct chain · 39% helix, 17% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Alanine DEHYDROGENASE/PYRIDINE nucleotide transhydrogenase (EC 1.4.1.1)	protein	345	39% helix, 17% strand	A0QNT0

Ligands and binding sites

CA · Calcium ion · metal · 3 copies · chains A
NA · Sodium ion · metal · chains A
EDO · 1,2-ethanediol · additive · 2 copies · 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	711	0.72	0.78	57	empty

Compared structures

3P2Y · Crystal structure of alanine dehydrogenase/pyridine nucleotide transhydrogenase from… · 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 A0QNT0
Elsewhere: RCSB PDB 3P2Y · PDBe 3P2Y · UniProt A0QNT0

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