MolNFT v1 · #180607 · protein

Crystal structure of the dark-adapted full-length bacteriophytochrome xccbphp-G454E variant from xanthomonas campestris in the pfr state

7L59: “Crystal structure of the dark-adapted full-length bacteriophytochrome xccbphp-G454E variant from xanthomonas…”. X-ray diffraction, 1 ligand (BLA), 7 pockets (best druggability 0.80). MolNFT v1 #180607 on GenesisL1: 3D structure…

PDB: 7L59
Type: protein
Length: 600 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Bacteriophytochrome
UniProt: A0A0H2XCS3
Ligands: BLA
Pockets: 7 · best druggability 0.80

Structure

x-ray diffraction · 1 distinct chain · 34% helix, 22% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Bacteriophytochrome	protein	600	34% helix, 22% strand	A0A0H2XCS3

Ligands and binding sites

BLA · Biliverdine IX alpha · ligand · chains A

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

Pockets

7 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	372	0.80	0.89	44	BLA
2	412	0.58	0.75	43	empty
3	218	0.57	0.79	19	empty
4	167	0.48	0.77	19	empty
5	63	0.43	0.82	17	empty

Modifications

Observed in the structure: 1 cofactor (biliverdin attachment).

Compared structures

7L59 · Crystal structure of the dark-adapted full-length bacteriophytochrome XccBphP-G454E… · 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 A0A0H2XCS3
Elsewhere: RCSB PDB 7L59 · PDBe 7L59 · UniProt A0A0H2XCS3

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