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Crystal structure of human granzyme H with a peptidyl substrate

Analyse Crystal structure of human granzyme H with a peptidyl substrate in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3TJV
Type: protein
Length: 234 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Granzyme H; Ptsyagddsg
EC: 3.4.21.-
UniProt: P20718
Ligands: SO4

Structure

x-ray diffraction · 2 distinct chains · 10% helix, 40% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Granzyme H (EC 3.4.21.-)	protein	225	10% helix, 40% strand	P20718
B	Ptsyagddsg	protein	9	0% helix, 44% strand	—

Ligands and binding sites

SO4 · Sulfate ion · ion · 2 copies · chains A

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

Interfaces

1 interface between chains.

A–B · 793 Å² buried · 20 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 3 disulfide (disulfide).

Compared structures

3TJV · Crystal structure of human granzyme H with a peptidyl substrate · the same entry in another collection · chain A against A, TM-score 1.00
P20718 · AlphaFold monomer V2.0 prediction for granzyme H (P20718) · 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 P20718
Elsewhere: RCSB PDB 3TJV · PDBe 3TJV · UniProt P20718

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