MolNFT v1 · #15594 · protein

Crystal structure of the bromide adduct of apha class B acid PHOSPHATASE/PHOSPHOTRANSFERASE from E. COLI at 2.2 a resolution

1N9K: “Crystal structure of the bromide adduct of apha class B acid PHOSPHATASE/PHOSPHOTRANSFERASE from E. COLI at…”. X-ray diffraction, 2 ligands (MG, BR), 4 pockets (best druggability 0.56). MolNFT v1 #15594 on GenesisL1: 3D structure…

PDB: 1N9K
Type: protein
Length: 418 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Class B acid phosphatase
EC: 3.1.3.2
UniProt: P32697
Ligands: MG, BR
Pockets: 4 · best druggability 0.56

Structure

x-ray diffraction · 1 distinct chain · 36% helix, 16% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Class B acid phosphatase (EC 3.1.3.2)	protein	209	36% helix, 16% strand	P32697

Ligands and binding sites

MG · Magnesium ion · metal · 2 copies · chains A, B
BR · Bromide ion · ion · 15 copies · chains A, B

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	238	0.56	0.78	30	MG, BR
2	222	0.55	0.78	30	BR
3	111	0.38	0.75	21	empty
4	103	0.35	0.74	20	empty

Interfaces

1 interface between chains.

A–B · 646 Å² buried · 7 hydrogen bonds · protein-protein

Compared structures

1N9K · Crystal structure of the bromide adduct of AphA class B acid… · 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 P32697
Elsewhere: RCSB PDB 1N9K · PDBe 1N9K · UniProt P32697

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