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Crystal structure of full-length split GFP mutant K26C disulfide dimer, P 21 21 21 space group

Analyse Crystal structure of full-length split GFP mutant K26C disulfide dimer, P 21 21… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
4W6C
Type
protein
Length
441 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Fluorescent protein D21H/K26C
Ligands
CRO
Pockets
3 · best druggability 0.81

Structure

x-ray diffraction · 2 distinct chains · 10% helix, 53% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AFluorescent protein D21H/K26Cprotein2189% helix, 54% strand—
BFluorescent protein D21H/K26Cprotein22310% helix, 52% strand—

Ligands and binding sites

  • CRO · {2-[(1R,2R)-1-amino-2-hydroxypropyl]-4-(4-hydroxybenzylidene)-5-oxo-4,5-dihydro-1H-imidazol-1-yl}acetic acid · ligand · 2 copies · chains A, B

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

Pockets

3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11320.810.9833CRO
21040.790.9826CRO
31340.400.7421empty

Interfaces

1 interface between chains.

  • A–B · 326 Ų buried · 3 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 4 cofactor, 1 disulfide (chromophore, disulfide).

Compared structures

  • 4W6C · Crystal Structure of Full-Length Split GFP Mutant K26C Disulfide Dimer, P 21 21 21 Space… · the same entry in another collection · chain A against A, TM-score 1.00

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