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Crystal structure of the novel secretory signalling protein from porcine (spp-40) at 2.1A resolution.

Analyse Crystal structure of the novel secretory signalling protein from porcine… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1XRV
Type: protein
Length: 361 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Signal processing protein
Ligands: NAG
Pockets: 3 · best druggability 0.53

Structure

x-ray diffraction · 1 distinct chain · 36% helix, 24% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Signal processing protein	protein	361	36% helix, 24% strand	—

Ligands and binding sites

NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 2 copies · chains A

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

Pockets

3 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	117	0.53	0.82	22	empty
2	185	0.53	0.78	25	empty
3	106	0.40	0.76	19	empty

Modifications

Observed in the structure: 2 disulfide, 1 glycan (disulfide, N-glycosylation).

Compared structures

1XRV · Crystal Structure of the novel secretory signalling protein from Porcine (SPP-40) at 2.1A… · 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 1XRV · PDBe 1XRV

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