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Ligands
Code Name Style Show Link
0DS N-{(2r)-2-[2-(hydroxyamino)-2-oxoethyl]-4-methylpentanoyl}-L-leucyl-L-phenylalaninamide
CA Calcium ion
ZN Zinc ion
Non-standard Residues
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Glycosylation
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Code : 1UMT   PDBj   RCSB PDB   PDBe
Header : HYDROLASE/HYDROLASE INHIBITOR
Title : Stromelysin-1 catalytic domain with hydrophobic inhibitor bound, pH 7.0, 32oc, 20 mm cacl2, 15% acetonitrile; NMR average of 20 structures minimized with restraints
Release Data : 1996-03-08
Compound :
mol_id molecule chains synonym
1 STROMELYSIN-1 A MATRIX METALLOPROTEINASE-3, MMP-3
ec: 3.4.24.17
fragment: CATALYTIC DOMAIN RESIDUES 83 - 256
Source :
mol_id organism_scientific organism_common expression_system
1 Homo sapiens  (taxid:9606) Human Escherichia coli  (taxid:562)
gene: HUMAN STROMELYSIN-1 CATALYTIC
expression_system_plasmid: PGEMEX-D
expression_system_gene: HUMAN STROMELYSIN-1 CATALYTIC DOMAIN
other_details: INDUCTION BY M13 WITH T7 RNA POLYMERASE
Authors : Van Doren, S.R., Kurochkin, A.V., Hu, W., Zuiderweg, E.R.P.
Keywords : ZINC HYDROLASE, METZINCIN, MATRIX METALLOPROTEINASE, HYDROLASE-HYDROLASE INHIBITOR COMPLEX
Exp. method : SOLUTION NMR
Citation :

Solution structure of the catalytic domain of human stromelysin complexed with a hydrophobic inhibitor.

Van Doren, S.R.,Kurochkin, A.V.,Hu, W.  et al.
(1995)  Protein Sci.  4 : 2487 - 2498

PubMed: 8580839

Assignments for the Main-Chain Nuclear Magnetic Resonances and Delineation of the Secondary Structure of the Catalytic Domain of Human Stromelysin-1 as Obtained from Triple-Resonance 3D NMR Experiments

Van Doren, S.R.,Kurochkin, A.V.,Ye, Q.-Z.  et al.
(1993)  Biochemistry  32 : 13109

Chain : A
UniProt : P08254 (MMP3_HUMAN)
Reaction: EC: Evidence:
Physiological Direction:
Preferential cleavage where P1', P2' and P3' are hydrophobic residues. 3.4.24.17 PubMed:1371271, PubMed:21330369
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