1Q3A: Stromelysin-2

Crystal structure of the catalytic domain of human matrix metalloproteinase 10. Determined by X-ray diffraction at 2.1 Å resolution. Released 6 Apr 2004.

Method: X-ray diffraction
Resolution: 2.1 Å
Organism: Homo sapiens
Chains: 3
Atoms: 4,175
Mol. weight: 57.31 kDa
Ligands: CA, NGH, ZN
Released: 6 Apr 2004

Explore 1Q3A in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1Q3A contains 10 α-helices and 21 β-strands across 3 chains. 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: 4 helices, 7 β-strands

Element	Residues	Length	Sheet
β-strand	112-117	6	1
α-helix	126-141	16
β-strand	147-151	5	1
β-strand	158-163	6	1
β-strand	181-183	3	1
α-helix	184-185	2
β-strand	194-197	4	1
β-strand	202-203	2	2
β-strand	209-210	2	2
α-helix	211-223	13
α-helix	252-262	11

Chain B: 3 helices, 7 β-strands

Element	Residues	Length	Sheet
β-strand	112-117	6	3
α-helix	126-142	17
β-strand	147-150	4	3
β-strand	158-163	6	3
β-strand	181-183	3	3
β-strand	194-197	4	3
β-strand	202-203	2	4
β-strand	209-210	2	4
α-helix	211-222	12
α-helix	252-262	11

Chain C: 3 helices, 7 β-strands

Element	Residues	Length	Sheet
β-strand	112-117	6	5
α-helix	126-141	16
β-strand	147-150	4	5
β-strand	158-163	6	5
β-strand	181-183	3	5
β-strand	194-197	4	5
β-strand	202-203	2	6
β-strand	209-210	2	6
α-helix	211-222	12
α-helix	252-262	11

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Stromelysin-2	A, B, C	protein	165	Homo sapiens	P09238 (AlphaFold model)

Sequence of entity 1 (A, B, C), FASTA

>1Q3A_1 Stromelysin-2 (chains A, B, C)
FSSFPGMPKWRKTHLTYRIVNYTPDLPRDAVDSAIEKALKVWEEVTPLTFSRLYEGEADI
MISFAVKEHGDNYSFDGPGHSLAHAYPPGPGLYGDIHFDDDEKWTEDASGTNLFLVAAHE
LGHSLGLFHSANTEALMYPLYNSFTELAQFRLSQDDVNGIQSLYG

Ligands and cofactors

ID	Name	Formula	Copies
CA	Calcium ion	Ca	9
NGH	N-isobutyl-N-[4-methoxyphenylsulfonyl]glycyl hydroxamic acid	C13 H20 N2 O5 S	3
ZN	Zinc ion	Zn	6

Primary citation

Crystal structure of the catalytic domain of human matrix metalloproteinase 10. Bertini, I., Calderone, V., Fragai, M. et al. J Mol Biol (2004) 336:707-716. DOI 10.1016/j.jmb.2003.12.033 · PubMed

Other PDB entries of the same protein (UniProt P09238 (AlphaFold model), which also has an AlphaFold model), best resolution first:

9CSX 1.67 Å, matrix metalloproteinase-10 proenzyme
3V96 1.9 Å, Complex of matrix metalloproteinase-10 catalytic domain (MMP-10cd) with tissue inhibitor…
4ILW 2.1 Å, Complex of matrix metalloproteinase-10 catalytic domain (MMP-10cd) with tissue inhibitor…

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