1IAU

HUMAN GRANZYME B IN COMPLEX WITH AC-IEPD-CHO

Summary for 1IAU

• Entry DOI: 10.2210/pdb1iau/pdb
• Related: 1FI8 1FQ3
• Related PRD ID: PRD_000300
• Descriptor: GRANZYME B, acetyl-isoleucyl-glutamyl-prolyl-aspartyl-aldehyde peptide INHIBITOR, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-[beta-D-mannopyranose-(1-6)]alpha-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-[alpha-L-fucopyranose-(1-6)]2-acetamido-2-deoxy-beta-D-glucopyranose, ... (6 entities in total)
• Functional Keywords: hydrolase-hydrolase inhibitor complex, hydrolase/hydrolase inhibitor
• Biological source: Homo sapiens (human); More
• Cellular location: Cytoplasmic granule: P10144
• Total number of polymer chains: 2
• Total formula weight: 27713.42

Authors

Rotonda, J.,Garcia-Calvo, M.,Bull, H.G.,Geissler, W.M.,McKeever, B.M.,Willoughby, C.A.,Thornberry, N.A.,Becker, J.W. (deposition date: 2001-03-23, release date: 2001-05-02, Last modification date: 2023-11-15)

Primary citation

Rotonda, J.,Garcia-Calvo, M.,Bull, H.G.,Geissler, W.M.,McKeever, B.M.,Willoughby, C.A.,Thornberry, N.A.,Becker, J.W.
The three-dimensional structure of human granzyme B compared to caspase-3, key mediators of cell death with cleavage specificity for aspartic acid in P1.
Chem.Biol., 8:357-368, 2001

PubMed Abstract: Granzyme B, one of the most abundant granzymes in cytotoxic T-lymphocyte (CTL) granules, and members of the caspase (cysteine aspartyl proteinases) family have a unique cleavage specificity for aspartic acid in P1 and play critical roles in the biochemical events that culminate in cell death.

PubMed: 11325591
DOI: 10.1016/S1074-5521(01)00018-7

Experimental method

X-RAY DIFFRACTION (2 Å)