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Crystal structure of non-specific class-C acid phosphatase from sphingobium sp. rsms bound to adenosine at pH 5.5

Analyse Crystal structure of non-specific class-C acid phosphatase from sphingobium sp.… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7F7C
Type: protein
Length: 254 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Acid phosphatase
UniProt: A0A197BYF0
Ligands: ADN, MG, PO4
Pockets: 3 · best druggability 0.57

Structure

x-ray diffraction · 1 distinct chain · 43% helix, 18% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Acid phosphatase	protein	254	43% helix, 18% strand	A0A197BYF0

Ligands and binding sites

ADN · Adenosine · ligand · chains A
MG · Magnesium ion · metal · chains A
PO4 · Phosphate ion · ion · 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	330	0.57	0.76	34	ADN, PO4, MG
2	212	0.48	0.75	20	empty
3	55	0.33	0.77	14	empty

Modifications

Observed in the structure: 1 disulfide (disulfide).

Compared structures

7F7C · Crystal structure of Non-specific class-C acid phosphatase from Sphingobium sp. RSMS… · 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 A0A197BYF0
Elsewhere: RCSB PDB 7F7C · PDBe 7F7C · UniProt A0A197BYF0

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