1SLM: Stromelysin-1

Crystal structure of fibroblast stromelysin-1: the C-truncated human proenzyme. Determined by X-ray diffraction at 1.9 Å resolution. Released 17 Dec 1996.

Method
X-ray diffraction
Resolution
1.9 Å
Organism
Homo sapiens
Chains
1
Atoms
1,927
Mol. weight
29.03 kDa
Ligands
ZN, CA
Released
17 Dec 1996

Explore 1SLM in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1SLM contains 7 α-helices and 10 β-strands across 1 chain. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.

Chain A: 7 helices, 10 β-strands

ElementResiduesLengthSheet
α-helix17-248
α-helix41-5313
α-helix64-696
β-strand7411
β-strand96-10162
α-helix110-12516
β-strand131-13442
β-strand142-14762
β-strand16311
β-strand165-16732
β-strand178-18142
β-strand186-18723
β-strand193-19423
α-helix195-20612
β-strand22211
α-helix229-2313
α-helix236-24611

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Stromelysin-1Aprotein255Homo sapiensP08254 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>1SLM_1 STROMELYSIN-1 (chains A)
YPLDGAARGEDTSMNLVQKYLENYYDLKKDVKQFVRRKDSGPVVKKIREMQKFLGLEVTG
KLDSDTLEVMRKPRCGVPDVGHFRTFPGIPKWRKTHLTYRIVNYTPDLPKDAVDSAVEKA
LKVWEEVTPLTFSRLYEGEADIMISFAVREHGDFYPFDGPGNVLAHAYAPGPGINGDAHF
DDDEQWTKDTTGTNLFLVAAHEIGHSLGLFHSANTEALMYPLYHSLTDLTRFRLSQDDIN
GIQSLYGPPPDSPET

Ligands and cofactors

IDNameFormulaCopies
ZNZinc ionZn2
CACalcium ionCa2

Primary citation

Stromelysin-1: three-dimensional structure of the inhibited catalytic domain and of the C-truncated proenzyme. Becker, J.W., Marcy, A.I., Rokosz, L.L. et al. Protein Sci (1995) 4:1966-1976. PubMed

Other PDB entries of the same protein (UniProt P08254 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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