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Solution NMR structure of the phycobilisome linker polypeptide domain of cpcc (20-153) from thermosynechococcus elongatus, northeast structural genomics consortium target TER219A

Analyse Solution NMR structure of the phycobilisome linker polypeptide domain of cpcc… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2L8V
Type: protein
Length: 143 residues
Chains: 1
Method: solution nmr
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Phycobilisome 32.1 kda linker polypeptide, phycocyanin- associated, rod
UniProt: P50034
Pockets: 2 · best druggability 0.57

Structure

solution nmr · 1 distinct chain · 50% helix, 3% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Phycobilisome 32.1 kda linker polypeptide, phycocyanin- associated, rod	protein	143	50% helix, 3% strand	P50034

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	152	0.57	0.82	19	empty
2	68	0.32	0.75	15	empty

Compared structures

2L8V · Solution NMR structure of the phycobilisome linker polypeptide domain of CpcC (20-153)… · the same entry in another collection · chain A against A, TM-score 1.00
P50034 · AlphaFold monomer V2.0 prediction for phycobilisome 32.1 kda linker polypeptide… · a predicted model of the same protein · chain A against A, TM-score 0.80

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 P50034
Elsewhere: RCSB PDB 2L8V · PDBe 2L8V · UniProt P50034

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