Research workbench

Co-complex structure of achromobactin synthetase protein D (acsd) with citrate in ATP binding site from pectobacterium chrysanthemi

Analyse Co-complex structure of achromobactin synthetase protein D (acsd) with citrate… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2W04
Type: protein
Length: 1,150 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Acsd
UniProt: Q93AT8
Pockets: 3 · best druggability 0.83

Structure

x-ray diffraction · 2 distinct chains · 45% helix, 19% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Acsd	protein	575	46% helix, 19% strand	Q93AT8
B	Acsd	protein	575	44% helix, 20% strand	Q93AT8

Ligands and binding sites

FLC · Citrate anion · additive · chains 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, 3 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	650	0.83	0.88	99	empty
2	492	0.82	0.89	88	FLC
3	493	0.71	0.80	66	empty

Interfaces

1 interface between chains.

A–B · 862 Å² buried · 3 hydrogen bonds · protein-protein

Compared structures

2W04 · Co-complex Structure of Achromobactin Synthetase Protein D (AcsD) with citrate in ATP… · 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 Q93AT8
Elsewhere: RCSB PDB 2W04 · PDBe 2W04 · UniProt Q93AT8

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.