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Crystal structure of SDSA1, an alkylsulfatase from pseudomonas aeruginosa, in complex with 1-dodecanol

Analyse Crystal structure of SDSA1, an alkylsulfatase from pseudomonas aeruginosa, in… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2CFZ
Type: protein
Length: 630 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Sds hydrolase SDSA1
UniProt: Q9I5I9
Ligands: 1DO, ZN
Pockets: 3 · best druggability 0.77

Structure

x-ray diffraction · 1 distinct chain · 42% helix, 16% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Sds hydrolase SDSA1	protein	630	42% helix, 16% strand	Q9I5I9

Ligands and binding sites

1DO · 1-dodecanol · ligand · chains A
ZN · Zinc ion · metal · 2 copies · chains A
PEG · Di(hydroxyethyl)ether · additive · 3 copies · 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, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	943	0.77	0.79	77	1DO
2	934	0.73	0.76	54	empty
3	70	0.39	0.78	12	empty

Compared structures

2CFZ · Crystal structure of SdsA1, an alkylsulfatase from Pseudomonas aeruginosa, in complex… · 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 Q9I5I9
Elsewhere: RCSB PDB 2CFZ · PDBe 2CFZ · UniProt Q9I5I9

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