MolNFT v1 · #172556 · protein

Structure of PCC2 from pyrococcus abyssi

7A66: “Structure of PCC2 from pyrococcus abyssi”. X-ray diffraction, 2 pockets (best druggability 0.47). MolNFT v1 #172556 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 7A66
Type: protein
Length: 255 residues
Chains: 3
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: PCC2
Pockets: 2 · best druggability 0.47

Structure

x-ray diffraction · 2 distinct chains · 47% helix, 34% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	PCC2	protein	83	48% helix, 34% strand	—
B, C	PCC2	protein	86	47% helix, 35% strand	—

Ligands and binding sites

GOL · Glycerol · additive · 5 copies · chains A, B, C

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

Pockets

2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	179	0.47	0.75	30	GOL
2	66	0.29	0.74	16	GOL

Interfaces

2 interfaces between chains.

A–C · 777 Å² buried · 10 hydrogen bonds · protein-protein
A–B · 777 Å² buried · 8 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 2 modified (phosphorylation).

Compared structures

7A66 · structure of Pcc2 from Pyrococcus abyssi · 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 7A66 · PDBe 7A66

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