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Crystal structure of ATU3015, a putative cytidylate kinase from agrobacterium tumefaciens, northeast structural genomics target ATR62

Analyse Crystal structure of ATU3015, a putative cytidylate kinase from agrobacterium… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1ZP6
Type: protein
Length: 176 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Hypothetical protein ATU3015
UniProt: Q8UBK1
Ligands: SO4
Pockets: 3 · best druggability 0.72

Structure

x-ray diffraction · 1 distinct chain · 39% helix, 14% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Hypothetical protein ATU3015	protein	176	39% helix, 14% strand	Q8UBK1

Ligands and binding sites

SO4 · Sulfate 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	379	0.72	0.84	43	SO4
2	90	0.42	0.79	15	empty
3	51	0.25	0.73	14	empty

Modifications

Observed in the structure: 2 modified (engineered).

Compared structures

1ZP6 · Crystal Structure of Atu3015, a Putative Cytidylate Kinase from Agrobacterium… · 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 Q8UBK1
Elsewhere: RCSB PDB 1ZP6 · PDBe 1ZP6 · UniProt Q8UBK1

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