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Crystal structure of putative kinase from clostridium symbiosum atcc 14940

Analyse Crystal structure of putative kinase from clostridium symbiosum atcc 14940 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3HDT
Type: protein
Length: 338 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Putative kinase
Ligands: PO4, CL
Pockets: 4 · best druggability 0.50

Structure

x-ray diffraction · 1 distinct chain · 58% helix, 15% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Putative kinase	protein	169	58% helix, 15% strand	—

Ligands and binding sites

PO4 · Phosphate ion · ion · 2 copies · chains A, B
CL · Chloride ion · ion · 2 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, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	143	0.50	0.79	26	PO4, CL
2	86	0.41	0.78	14	PO4
3	66	0.35	0.77	14	empty
4	55	0.34	0.78	12	CL

Interfaces

1 interface between chains.

A–B · 1078 Å² buried · 14 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 8 modified (engineered).

Compared structures

3HDT · Crystal structure of putative kinase from Clostridium symbiosum ATCC 14940 · 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
Elsewhere: RCSB PDB 3HDT · PDBe 3HDT

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