966C: MMP-1

Crystal structure of fibroblast collagenase-1 complexed to a diphenyl-ether sulphone based hydroxamic acid. Determined by X-ray diffraction at 1.9 Å resolution. Released 7 Aug 1999.

Method
X-ray diffraction
Resolution
1.9 Å
Organism
Homo sapiens
Chains
1
Atoms
1,405
Mol. weight
18.26 kDa
Ligands
RS2, CA, ZN
Released
7 Aug 1999

Explore 966C in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

966C contains 3 α-helices and 9 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: 3 helices, 9 β-strands

ElementResiduesLengthSheet
β-strand113-11861
α-helix127-14216
β-strand148-15141
β-strand159-16461
β-strand16812
β-strand17012
β-strand182-18431
β-strand195-19841
β-strand20413
β-strand21113
α-helix212-22312
α-helix250-26011

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
MMP-1Aprotein157Homo sapiensP03956 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>966C_1 MMP-1 (chains A)
RWEQTHLTYRIENYTPDLPRADVDHAIEKAFQLWSNVTPLTFTKVSEGQADIMISFVRGD
HRDNSPFDGPGGNLAHAFQPGPGIGGDAHFDEDERWTNNFREYNLHRVAAHELGHSLGLS
HSTDIGALMYPSYTFSGDVQLAQDDIDGIQAIYGRSQ

Ligands and cofactors

IDNameFormulaCopies
RS2N-hydroxy-2-[4-(4-phenoxy-benzenesulfonyl)-tetrahydro-pyran-4-yl]-acetamideC19 H21 N O6 S1
CACalcium ionCa3
ZNZinc ionZn2

Primary citation

Crystal structures of MMP-1 and -13 reveal the structural basis for selectivity of collagenase inhibitors. Lovejoy, B., Welch, A.R., Carr, S. et al. Nat Struct Biol (1999) 6:217-221. DOI 10.1038/6657 · PubMed

Other PDB entries of the same protein (UniProt P03956 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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