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Crystal structure of baculovirus P35

Analyse Crystal structure of baculovirus P35 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1P35
Type: protein
Length: 892 residues
Chains: 3
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: P35
UniProt: P08160
Ligands: PO4
Pockets: 10 · best druggability 0.67

Structure

x-ray diffraction · 3 distinct chains · 17% helix, 41% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	P35	protein	299	18% helix, 41% strand	P08160
B	P35	protein	298	16% helix, 41% strand	P08160
C	P35	protein	295	17% helix, 42% strand	P08160

Ligands and binding sites

PO4 · Phosphate ion · ion · 3 copies · chains A, C, B
EDO · 1,2-ethanediol · additive · 3 copies · chains A, B

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	672	0.67	0.76	66	empty
2	508	0.60	0.74	47	empty
3	234	0.59	0.80	29	empty
4	71	0.57	0.88	18	empty
5	160	0.57	0.82	29	empty

Interfaces

2 interfaces between chains.

A–C · 723 Å² buried · 11 hydrogen bonds · protein-protein
B–C · 313 Å² buried · 2 hydrogen bonds · protein-protein

Compared structures

1P35 · Crystal structure of baculovirus P35 · 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 P08160
Elsewhere: RCSB PDB 1P35 · PDBe 1P35 · UniProt P08160

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