MolNFT v1 · #3457 · protein

Alpha-fluoro acid and alpha-fluoro amide analogs of acetyl-CoA as inhibitors of of citrate synthase: effect of PKA matching on binding affinity and hydrogen bond length

1CSS: “Alpha-fluoro acid and alpha-fluoro amide analogs of acetyl-CoA as inhibitors of of citrate synthase: effect…”. X-ray diffraction, 2 ligands (OAA, FCX), 3 pockets (best druggability 0.67). MolNFT v1 #3457 on GenesisL1: 3D structure…

PDB: 1CSS
Type: protein
Length: 435 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Citrate synthase
EC: 4.1.3.7
UniProt: P23007
Ligands: OAA, FCX
Pockets: 3 · best druggability 0.67

Structure

x-ray diffraction · 1 distinct chain · 63% helix, 3% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Citrate synthase (EC 4.1.3.7)	protein	435	63% helix, 3% strand	P23007

Ligands and binding sites

OAA · Oxaloacetate ion · ligand · chains A
FCX · Alpha-fluoro-carboxymethyldethia coenzyme A complex · ligand · chains A

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

Pockets

3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	544	0.67	0.77	54	OAA, FCX
2	75	0.36	0.76	8	empty
3	75	0.32	0.74	13	empty

Compared structures

1CSS · Alpha-fluoro acid and alpha-fluoro amide analogs of acetyl-CoA as inhibitors of of… · 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 P23007
Elsewhere: RCSB PDB 1CSS · PDBe 1CSS · UniProt P23007

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