MolNFT v1 · #144902 · protein

Crystal structure of aspartate semialdehyde dehydrogenase from blastomyces dermatitidis with P-benzoquinone

6C85 · Aspartate-semialdehyde dehydrogenase: “Crystal structure of aspartate semialdehyde dehydrogenase from blastomyces dermatitidis with P-benzoquinone”. X-ray diffraction, 1 ligand (PLQ), 3 pockets (best druggability 0.61). MolNFT v1…

PDB: 6C85
Type: protein
Length: 708 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Aspartate-semialdehyde dehydrogenase
UniProt: C5GC63
Ligands: PLQ
Pockets: 3 · best druggability 0.61

Structure

x-ray diffraction · 1 distinct chain · 31% helix, 23% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Aspartate-semialdehyde dehydrogenase	protein	354	31% helix, 23% strand	C5GC63

Ligands and binding sites

PLQ · 1,4-benzoquinone · 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	370	0.61	0.77	50	PLQ
2	327	0.60	0.78	42	PLQ
3	52	0.34	0.79	16	empty

Interfaces

1 interface between chains.

A–B · 1740 Å² buried · 37 hydrogen bonds · protein-protein

Compared structures

6C85 · Crystal structure of aspartate semialdehyde dehydrogenase from Blastomyces dermatitidis… · 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 C5GC63
Elsewhere: RCSB PDB 6C85 · PDBe 6C85 · UniProt C5GC63

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