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The crystal structure of an archaeal cpsf subunit, PH1404 from pyrococcus horikoshii

Analyse The crystal structure of an archaeal cpsf subunit, PH1404 from pyrococcus… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3AF5
Type: protein
Length: 638 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Putative uncharacterized protein PH1404
UniProt: O50112
Ligands: ZN, SO4
Pockets: 7 · best druggability 0.81

Structure

x-ray diffraction · 1 distinct chain · 37% helix, 21% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Putative uncharacterized protein PH1404	protein	638	37% helix, 21% strand	O50112

Ligands and binding sites

ZN · Zinc ion · metal · 4 copies · chains A
SO4 · Sulfate ion · ion · 6 copies · chains A
ACY · Acetic acid · additive · 4 copies · chains A

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

Pockets

7 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	169	0.81	0.96	30	SO4
2	975	0.76	0.79	92	ACY
3	419	0.63	0.77	51	empty
4	114	0.45	0.78	22	empty
5	76	0.41	0.79	19	empty

Compared structures

3AF5 · The crystal structure of an archaeal CPSF subunit, PH1404 from Pyrococcus horikoshii · 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 O50112
Elsewhere: RCSB PDB 3AF5 · PDBe 3AF5 · UniProt O50112

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