Research workbench

Structure of the novel 14 kda fragment of alpha-subunit of phycoerythrin from the starving cyanobacterium phormidium tenue

Analyse Structure of the novel 14 kda fragment of alpha-subunit of phycoerythrin from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3MWN
Type: protein
Length: 266 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Phycoerythrin
Ligands: CYC
Pockets: 5 · best druggability 0.63

Structure

x-ray diffraction · 1 distinct chain · 60% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Phycoerythrin	protein	133	60% helix, 0% strand	—

Ligands and binding sites

CYC · Phycocyanobilin · ligand · 4 copies · chains A, B

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	157	0.63	0.85	30	CYC
2	154	0.51	0.79	31	CYC
3	106	0.48	0.80	16	empty
4	89	0.45	0.80	16	empty
5	83	0.42	0.79	14	empty

Interfaces

1 interface between chains.

A–B · 117 Å² buried · 4 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 4 cofactor (phycocyanobilin attachment).

Compared structures

3MWN · Structure of the Novel 14 kDa Fragment of alpha-Subunit of Phycoerythrin from the… · 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 3MWN · PDBe 3MWN

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.