MolNFT v1 · #141639 · protein

Crystal structure of kluyveromyces polyspora adh (kpadh) mutant (E214V/T215S)

5ZED · Uncharacterized protein adh: “Crystal structure of kluyveromyces polyspora adh (kpadh) mutant (E214V/T215S)”. X-ray diffraction, 1 ligand (NAP), 3 pockets (best druggability 0.76). MolNFT v1 #141639 on GenesisL1: 3D structure…

PDB: 5ZED
Type: protein
Length: 684 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Uncharacterized protein adh
UniProt: A7TM80
Ligands: NAP
Pockets: 3 · best druggability 0.76

Structure

x-ray diffraction · 1 distinct chain · 43% helix, 15% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Uncharacterized protein adh	protein	342	43% helix, 15% strand	A7TM80

Ligands and binding sites

NAP · Nadp nicotinamide-adenine-dinucleotide phosphate · ligand · 2 copies · chains A, B

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

Pockets

3 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	584	0.76	0.82	56	NAP
2	618	0.76	0.82	68	NAP
3	117	0.38	0.74	18	empty

Interfaces

1 interface between chains.

A–B · 192 Å² buried · 4 hydrogen bonds · protein-protein

Compared structures

5ZED · Crystal structure of Kluyveromyces polyspora ADH (KpADH) mutant (E214V/T215S) · 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 A7TM80
Elsewhere: RCSB PDB 5ZED · PDBe 5ZED · UniProt A7TM80

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