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Structure of S-type phycobiliprotein lyase cpes from guillardia theta

Analyse Structure of S-type phycobiliprotein lyase cpes from guillardia theta in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4TQ2
Type: protein
Length: 177 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Putative phycoerythrin lyase
UniProt: L1JFC7
Pockets: 1 · best druggability 0.73

Structure

x-ray diffraction · 1 distinct chain · 15% helix, 55% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Putative phycoerythrin lyase	protein	177	15% helix, 55% strand	L1JFC7

Ligands and binding sites

HEZ · Hexane-1,6-diol · additive · 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	551	0.73	0.81	47	HEZ

Compared structures

4TQ2 · Structure of S-type Phycobiliprotein Lyase CPES from Guillardia theta · 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 L1JFC7
Elsewhere: RCSB PDB 4TQ2 · PDBe 4TQ2 · UniProt L1JFC7

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