MolNFT v1 · #67371 · protein

1.95 ångström crystal structure of COCE/NOND family hydrolase (SACOL2612) from staphylococcus aureus

3III: “1.95 ångström crystal structure of COCE/NOND family hydrolase (SACOL2612) from staphylococcus aureus”. X-ray diffraction, 3 ligands (PLM, NI, CL), 4 pockets (best druggability 0.71). MolNFT v1 #67371 on GenesisL1: 3D structure…

PDB: 3III
Type: protein
Length: 556 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: COCE/NOND family hydrolase
UniProt: Q5HCV6
Ligands: PLM, NI, CL
Pockets: 4 · best druggability 0.71

Structure

x-ray diffraction · 1 distinct chain · 21% helix, 35% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	COCE/NOND family hydrolase	protein	556	21% helix, 35% strand	Q5HCV6

Ligands and binding sites

PLM · Palmitic acid · ligand · chains A
NI · Nickel (II) ion · metal · chains A
CL · Chloride ion · ion · 4 copies · chains A

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	50	0.71	0.99	19	empty
2	464	0.70	0.80	42	PLM
3	99	0.38	0.76	21	empty
4	56	0.30	0.75	13	empty

Modifications

Observed in the structure: 12 modified (engineered).

Compared structures

3III · 1.95 Angstrom Crystal Structure of CocE/NonD family hydrolase (SACOL2612) from… · 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 Q5HCV6
Elsewhere: RCSB PDB 3III · PDBe 3III · UniProt Q5HCV6

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