ISDA: 9MNB

Deposition Date 2024-12-20

Release Date 2026-04-22

Last Version Date 2026-04-22

Entry Detail

PDB ID:

9MNB

Keywords:

IMMUNE SYSTEM/Hydrolase

Title:

Beta1-tryptase monomer bound to inhibitory Fabs E82.AS and E104.v2

Biological Source:

Source Organism(s):

Homo sapiens (Taxon ID: 9606)
Lama glama (Taxon ID: 9844)

Expression System(s):

Homo sapiens, Trichoplusia ni

Method Details:

Experimental Method:

ELECTRON MICROSCOPY

Resolution:

3.00 Å

Aggregation State:

PARTICLE

Reconstruction Method:

SINGLE PARTICLE

Download Validation Report

Macromolecular Entities

Structures with similar UniProt ID

Protein Blast

Polymer Type:polypeptide(L)
Molecule:Tryptase alpha/beta-1
Gene (Uniprot):TPSAB1
Chain IDs:B (auth: A)
Chain Length:245
Number of Molecules:1
Biological Source:Homo sapiens

UniProt ID:Q15661 Pfam ID:PF00089 EC:3.4.21.59

Structures with similar UniProt ID

Protein Blast

Polymer Type:polypeptide(L)
Molecule:Heavy chain of E82.AS Fab
Chain IDs:E
Chain Length:216
Number of Molecules:1
Biological Source:Homo sapiens

UniProt ID:9MNB

Structures with similar UniProt ID

Protein Blast

Polymer Type:polypeptide(L)
Molecule:Light chain of E82.AS Fab
Chain IDs:D (auth: F)
Chain Length:220
Number of Molecules:1
Biological Source:Homo sapiens

UniProt ID:9MNB

Structures with similar UniProt ID

Protein Blast

Polymer Type:polypeptide(L)
Molecule:Heavy chain of E104v2 Fab
Chain IDs:C (auth: H)
Chain Length:221
Number of Molecules:1
Biological Source:Homo sapiens

UniProt ID:9MNB

Structures with similar UniProt ID

Protein Blast

Polymer Type:polypeptide(L)
Molecule:Anti-human kappa light chain
Chain IDs:F (auth: K)
Chain Length:120
Number of Molecules:1
Biological Source:Lama glama

UniProt ID:9MNB

Structures with similar UniProt ID

Protein Blast

Polymer Type:polypeptide(L)
Molecule:Light chain of E104.v2 Fab
Chain IDs:A (auth: L)
Chain Length:216
Number of Molecules:1
Biological Source:Homo sapiens

UniProt ID:9MNB

Ligand Molecules

Primary Citation

Complete inhibition of beta-tryptase by tetramer dissociation and active site allostery due to a single antibody residue.

Maun, H.R, Azumaya, C.M, Walters, B.T, Vij, R, Morando, A, Loyet, K.M, Koerber, J.T, Rohou, A, Lazarus, R.A.Show

Nat Commun 17 ? ? (2026)

PMID: 41957026 DOI: 10.1038/s41467-026-70491-3

Primary Citation of related structures

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