Research workbench

Dark, mutant H275T , 100K, pcm myxobacterial phytochrome, P2

Analyse Dark, mutant H275T , 100K, pcm myxobacterial phytochrome, P2 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6PU2
Type: protein
Length: 962 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Photoreceptor-histidine kinase bphp
UniProt: Q09E27
Ligands: EL5
Pockets: 9 · best druggability 0.82

Structure

x-ray diffraction · 1 distinct chain · 34% helix, 26% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Photoreceptor-histidine kinase bphp	protein	481	34% helix, 26% strand	Q09E27

Ligands and binding sites

EL5 · Biliverdin · ligand · 2 copies · chains A, B

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	370	0.82	0.91	46	EL5
2	377	0.82	0.91	48	EL5
3	129	0.66	0.88	30	empty
4	298	0.65	0.81	36	empty
5	161	0.59	0.83	26	empty

Interfaces

1 interface between chains.

A–B · 1827 Å² buried · 11 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 2 covalent (covalent ligand).

Compared structures

6PU2 · Dark, Mutant H275T , 100K, PCM Myxobacterial Phytochrome, P2 · 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 Q09E27
Elsewhere: RCSB PDB 6PU2 · PDBe 6PU2 · UniProt Q09E27

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