MolNFT v1 · #116036 · protein

Structure of cyclic nucleotide-binding-like protein from brucella abortus bv. 1 str. 9-941

5D1I · Cyclic nucleotide-binding protein: “Structure of cyclic nucleotide-binding-like protein from brucella abortus bv. 1 str. 9-941”. X-ray diffraction, 2 pockets (best druggability 0.44). MolNFT v1 #116036 on GenesisL1: 3D structure…

PDB: 5D1I
Type: protein
Length: 233 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Cyclic nucleotide-binding protein
UniProt: Q57AQ0
Pockets: 2 · best druggability 0.44

Structure

x-ray diffraction · 2 distinct chains · 27% helix, 39% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Cyclic nucleotide-binding protein	protein	117	27% helix, 40% strand	Q57AQ0
B	Cyclic nucleotide-binding protein	protein	116	27% helix, 38% strand	Q57AQ0

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	81	0.44	0.80	19	empty
2	51	0.37	0.80	20	empty

Interfaces

1 interface between chains.

A–B · 993 Å² buried · 15 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 2 modified (engineered).

Compared structures

5D1I · Structure of Cyclic nucleotide-binding-like protein from Brucella abortus bv. 1 str. 9-941 · 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 Q57AQ0
Elsewhere: RCSB PDB 5D1I · PDBe 5D1I · UniProt Q57AQ0

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