MolNFT v1 · #108458 · protein

Crystal structure of full-length split GFP mutant E124H/K126H with copper mediated crystal contacts, C 2 2 21 space group

4W7F · Fluorescent protein E124H/K126H: “Crystal structure of full-length split GFP mutant E124H/K126H with copper mediated crystal contacts, C 2 2 21…”. X-ray diffraction, 2 ligands (CRO, CU), 1 pocket (best druggability 0.84). MolNFT v1…

PDB: 4W7F
Type: protein
Length: 213 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Fluorescent protein E124H/K126H
Ligands: CRO, CU
Pockets: 1 · best druggability 0.84

Structure

x-ray diffraction · 1 distinct chain · 7% helix, 52% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Fluorescent protein E124H/K126H	protein	213	7% 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 · chains A
CU · Copper (II) ion · metal · chains A

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

Pockets

1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	218	0.84	0.96	37	CRO

Modifications

Observed in the structure: 1 cofactor (chromophore).

Compared structures

4W7F · Crystal Structure of Full-Length Split GFP Mutant E124H/K126H With Copper Mediated… · 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
Elsewhere: RCSB PDB 4W7F · PDBe 4W7F

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