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Identification of the serratia endonuclease dimer: structural basis and implications for catalysis

Analyse Identification of the serratia endonuclease dimer: structural basis and… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1SMN
Type: protein
Length: 482 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Extracellular endonuclease
EC: 3.1.30.2
UniProt: P13717
Pockets: 2 · best druggability 0.34

Structure

x-ray diffraction · 1 distinct chain · 27% helix, 22% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Extracellular endonuclease (EC 3.1.30.2)	protein	241	27% helix, 22% strand	P13717

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	79	0.34	0.75	21	empty
2	88	0.34	0.74	22	empty

Interfaces

1 interface between chains.

A–B · 921 Å² buried · 17 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 4 disulfide (disulfide).

Compared structures

1SMN · Identification of the serratia endonuclease dimer: structural basis and implications for… · the same entry in another collection · chain A against A, TM-score 1.00
P13717 · AlphaFold monomer V2.0 prediction for nuclease (P13717) · a predicted model of the same protein · 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 P13717
Elsewhere: RCSB PDB 1SMN · PDBe 1SMN · UniProt P13717

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