MolNFT v1 · #34030 · protein

Crystal structure of cytidine deaminase cdd-2 (BA4525) from bacillus anthracis at 2.40A resolution

2D30: “Crystal structure of cytidine deaminase cdd-2 (BA4525) from bacillus anthracis at 2.40A resolution”. X-ray diffraction, 1 ligand (ZN), 2 pockets (best druggability 0.48). MolNFT v1 #34030 on GenesisL1: 3D structure, binding sites…

PDB: 2D30
Type: protein
Length: 248 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Cytidine deaminase
EC: 3.5.4.5
UniProt: Q81LT6
Ligands: ZN
Pockets: 2 · best druggability 0.48

Structure

x-ray diffraction · 1 distinct chain · 32% helix, 27% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Cytidine deaminase (EC 3.5.4.5)	protein	124	32% helix, 27% strand	Q81LT6

Ligands and binding sites

ZN · Zinc ion · metal · 2 copies · chains A, B

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

2 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	192	0.48	0.76	26	empty
2	190	0.47	0.75	33	empty

Interfaces

1 interface between chains.

A–B · 383 Å² buried · 6 hydrogen bonds · protein-protein

Compared structures

2D30 · Crystal Structure of Cytidine Deaminase Cdd-2 (BA4525) from Bacillus Anthracis at 2.40A… · 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 Q81LT6
Elsewhere: RCSB PDB 2D30 · PDBe 2D30 · UniProt Q81LT6

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