MolNFT v2 · #155369 · protein

Crystal structure of Arabidopsis thaliana BIC2-CRY2 complex

6K8K: “Crystal structure of Arabidopsis thaliana BIC2-CRY2 complex”. X-ray diffraction at 2.5, 3 ligands (FAD, AMP, MG). MolNFT v2 #155369 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 6K8K
Type: protein
Length: 2,160 residues
Chains: 8
Method: x-ray diffraction
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 2.5
Source: Arabidopsis thaliana
UniProt: Q96524, Q9M280
Ligands: FAD, AMP, MG

Structure

x-ray diffraction · resolution 2.5 · 8 distinct chains.

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	—	protein	484	—	Q96524
E	—	protein	55	—	Q9M280
B	—	protein	481	—	Q96524
C	—	protein	51	—	Q9M280
D	—	protein	486	—	Q96524
F	—	protein	56	—	Q9M280
G	—	protein	490	—	Q96524
H	—	protein	57	—	Q9M280

Ligands and binding sites

FAD · Flavin-adenine dinucleotide · ligand · 4 copies · chains A, B, D, G
AMP · Adenosine monophosphate · ligand · 4 copies · chains A, B, D, G
MG · Magnesium ion · metal · 4 copies · chains A, D, F, G

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

Compared structures

6K8K · Crystal structure of arabidopsis thaliana BIC2-CRY2 complex · the same entry in another collection · chain H against H, TM-score 1.00
Q96524 · AlphaFold monomer V2.0 prediction for cryptochrome-2 (Q96524) · a predicted model of the same protein · chain D 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 Q96524
Every structure of UniProt Q9M280
Elsewhere: RCSB PDB 6K8K · PDBe 6K8K · UniProt Q96524 · UniProt Q9M280

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