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Structure of the S205A mutant of the cyan fluorescent protein cerulean at pH 7.0

Analyse Structure of the S205A mutant of the cyan fluorescent protein cerulean at pH 7.0 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5OXA
Type: protein
Length: 227 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Green fluorescent protein
UniProt: P42212
Ligands: B2H
Pockets: 1 · best druggability 0.77

Structure

x-ray diffraction · 1 distinct chain · 12% helix, 53% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Green fluorescent protein	protein	227	12% helix, 53% strand	P42212

Ligands and binding sites

B2H · Chromophore (thr, trp, gly) · ligand · 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	113	0.77	0.97	30	B2H

Modifications

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

Compared structures

5OXA · Structure of the S205A mutant of the Cyan Fluorescent Protein Cerulean at pH 7.0 · the same entry in another collection · chain A against A, TM-score 1.00
P42212 · AlphaFold monomer V2.0 prediction for green fluorescent protein (P42212) · a predicted model of the same protein · chain A against A, TM-score 0.99

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 P42212
Elsewhere: RCSB PDB 5OXA · PDBe 5OXA · UniProt P42212

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