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Crystal structure of aspartate semialdehyde dehydrogenase with NADP from blastomyces dermatitidis

Analyse Crystal structure of aspartate semialdehyde dehydrogenase with NADP from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6C8W
Type: protein
Length: 714 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Aspartate-semialdehyde dehydrogenase
UniProt: C5GC63
Ligands: NAP
Pockets: 4 · best druggability 0.71

Structure

x-ray diffraction · 1 distinct chain · 36% helix, 23% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Aspartate-semialdehyde dehydrogenase	protein	357	36% helix, 23% strand	C5GC63

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

4 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	558	0.71	0.80	61	NAP
2	537	0.66	0.77	58	NAP
3	50	0.30	0.77	15	empty
4	56	0.27	0.73	14	empty

Interfaces

1 interface between chains.

A–B · 1753 Å² buried · 35 hydrogen bonds · protein-protein

Compared structures

6C8W · Crystal structure of Aspartate Semialdehyde Dehydrogenase with NADP from Blastomyces… · the same entry in another collection · chain A against A, TM-score 1.00

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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 6C8W · PDBe 6C8W · UniProt C5GC63

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