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Trypsin from fusarium oxysporum- room temperature to atomic resolution

Analyse Trypsin from fusarium oxysporum- room temperature to atomic resolution in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1XVM
Type: protein
Length: 227 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Trypsin; Substrate tripeptide gly-ala-arg
EC: 3.4.21.4
UniProt: P35049

Structure

x-ray diffraction · 2 distinct chains · 11% helix, 37% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Trypsin (EC 3.4.21.4)	protein	224	12% helix, 38% strand	P35049
B	Substrate tripeptide gly-ala-arg	protein	3	0% helix, 33% strand	—

Interfaces

1 interface between chains.

A–B · 306 Å² buried · 14 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 3 disulfide (disulfide).

Compared structures

1XVM · Trypsin from Fusarium oxysporum- room temperature to atomic resolution · the same entry in another collection · chain A against A, TM-score 1.00
P35049 · AlphaFold monomer V2.0 prediction for trypsin (P35049) · 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 P35049
Elsewhere: RCSB PDB 1XVM · PDBe 1XVM · UniProt P35049

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