PDBsum entry 3d6h

Hydrolase/hydrolase inhibitor

PDB id: 3d6h

Contents

Protein chains

166 a.a. *

88 a.a. *

Ligands

PHQ-VAL-ALA-ASP-CF0

Waters ×180

* Residue conservation analysis

PDB id:

3d6h

Name:

Hydrolase/hydrolase inhibitor

Title:

Crystal structure of human caspase-1 with a naturally-occurring asn263->ser substitution in complex with 3-[2-(2- benzyloxycarbonylamino-3-methyl-butyrylamino)-propionylamino]-4-oxo- pentanoic acid (z-vad-fmk)

Structure:

Caspase-1. Chain: a. Fragment: caspase-1 subunit p20. Synonym: casp-1, interleukin-1 beta convertase, il-1bc, il-1 beta- converting enzyme, ice, interleukin-1 beta-converting enzyme, p45, caspase-1 subunit p20, caspase-1 subunit p10. Engineered: yes. Mutation: yes. Caspase-1 precursor.

Source:

Homo sapiens. Human. Organism_taxid: 9606. Gene: casp1, il1bc, il1bce. Expressed in: escherichia coli. Expression_system_taxid: 562. Synthetic: yes

Resolution:

2.00Å R-factor: 0.202 R-free: 0.237

Authors:

A.Rosen-Wolff,J.Roesler,M.J.Romanowski

Key ref:

A.Rosen-Wolff et al. Mutated, Structurally altered caspase-1 with decreased enzymatic and increased rip2-Meditated inflammatory activity leads to a new type of periodic fever (ice fever).. To be published, .

Date:

19-May-08 Release date: 02-Mar-10

Protein chain

P29466  (CASP1_HUMAN) -  Caspase-1 from Homo sapiens

Seq: 404 a.a.

Struc: 166 a.a.*

Protein chain

P29466  (CASP1_HUMAN) -  Caspase-1 from Homo sapiens

Seq: 404 a.a.

Struc: 88 a.a.

* PDB and UniProt seqs differ at 1 residue position (black cross)

Enzyme reactions

• Enzyme class: Chains A, B: E.C.3.4.22.36 - caspase-1.
• Reaction: Release of interleukin 1-beta by specific cleavage at 116-Asp-|-Ala-117 and 27-Asp-|-Gly-28 bonds in precursor. Also hydrolyzes the small- molecule substrate, Ac-Tyr-Val-Ala-Asp-|-NHMec.