MolNFT v1 · #123216 · protein

Bacillus cereus coth kinase plus MG2+/AMP

5JDA · Spore coat protein H: “Bacillus cereus coth kinase plus MG2+/AMP”. X-ray diffraction, 3 ligands (AMP, MG, NA), 4 pockets (best druggability 0.62). MolNFT v1 #123216 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 5JDA
Type: protein
Length: 359 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Spore coat protein H
EC: 2.7.11.1
UniProt: Q739M5
Ligands: AMP, MG, NA
Pockets: 4 · best druggability 0.62

Structure

x-ray diffraction · 1 distinct chain · 38% helix, 23% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Spore coat protein H (EC 2.7.11.1)	protein	359	38% helix, 23% strand	Q739M5

Ligands and binding sites

AMP · Adenosine monophosphate · ligand · chains A
MG · Magnesium ion · metal · 5 copies · chains A
NA · Sodium ion · metal · chains A
EDO · 1,2-ethanediol · additive · 10 copies · chains A
SIN · Succinic acid · additive · 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, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	297	0.62	0.80	44	AMP, MG, NA
2	76	0.48	0.83	17	EDO
3	81	0.45	0.81	14	EDO
4	53	0.31	0.76	12	SIN

Compared structures

5JDA · Bacillus cereus CotH kinase plus Mg2+/AMP · 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 Q739M5
Elsewhere: RCSB PDB 5JDA · PDBe 5JDA · UniProt Q739M5

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