1C3I: Human stromelysin-1 catalytic domain

Human stromelysin-1 catalytic domain complexed with ro-26-2812. Determined by X-ray diffraction at 1.83 Å resolution. Released 26 Jul 2000.

Method: X-ray diffraction
Resolution: 1.83 Å
Organism: Homo sapiens
Chains: 2
Atoms: 2,983
Mol. weight: 39.79 kDa
Ligands: ZN, CA, TR1
Released: 26 Jul 2000

Explore 1C3I in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1C3I contains 8 α-helices and 20 β-strands across 2 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: 5 helices, 10 β-strands

Element	Residues	Length	Sheet
β-strand	84-85	2	1
β-strand	96-101	6	2
β-strand	104	1	3
α-helix	110-125	16
β-strand	131-134	4	2
β-strand	142-147	6	2
β-strand	165-167	3	2
α-helix	168-169	2
β-strand	178-181	4	2
β-strand	186-187	2	4
β-strand	193-194	2	4
α-helix	195-206	12
β-strand	209-210	2	1
α-helix	223-226	4
α-helix	236-246	11

Chain B: 3 helices, 10 β-strands

Element	Residues	Length	Sheet
β-strand	85	1	5
β-strand	96-101	6	6
β-strand	104	1	3
α-helix	110-126	17
β-strand	131-134	4	6
β-strand	142-147	6	6
β-strand	165-167	3	6
β-strand	178-181	4	6
β-strand	186-187	2	7
β-strand	193-194	2	7
α-helix	195-206	12
β-strand	209	1	5
α-helix	236-246	11

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Stromelysin-1	A, B	protein	173	Homo sapiens	P08254 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>1C3I_1 STROMELYSIN-1 (chains A, B)
FRTFPGIPKWRKTHLTYRIVNYTPDLPKDAVDSAVEKALKVWEEVTPLTFSRLYEGEADI
MISFAVREHGDFYPFDGPGNVLAHAYAPGPGINGDAHFDDDEQWTKDTTGTNLFLVAAHE
IGHSLGLFHSANTEALMYPLYHSLTDLTRFRLSQDDINGIQSLYGPPPDSPET

Ligands and cofactors

ID	Name	Formula	Copies
ZN	Zinc ion	Zn	4
CA	Calcium ion	Ca	6
TR1	2-(2-{2-[(biphenyl-4-ylmethyl)-amino]-3-mercapto-pentanoylamino}-acetylamino)-3…	C24 H31 N3 O4 S	1

Primary citation

Expression, characterization and structure determination of an active site mutant (Glu202-Gln) of mini-stromelysin-1. Steele, D.L., El-Kabbani, O., Dunten, P. et al. Protein Eng (2000) 13:397-405. DOI 10.1093/protein/13.6.397 · PubMed

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

1HY7 1.5 Å, A carboxylic acid based inhibitor in complex with MMP3
1CIZ 1.64 Å, X-ray structure of human stromelysin catalytic domain complexes with non-peptide…
1HFS 1.7 Å, Crystal structure of the catalytic domain of human fibroblast stromelysin-1 inhibited…
1CAQ 1.8 Å, X-ray structure of human stromelysin catalytic domain complexes with non-peptide…
1USN 1.8 Å, Crystal structure of the catalytic domain of human fibroblast stromelysin-1 inhibited…
4G9L 1.88 Å, Structure of MMP3 complexed with NNGH inhibitor.
1G49 1.9 Å, A carboxylic acid based inhibitor in complex with MMP3
1SLM 1.9 Å, Crystal structure of fibroblast stromelysin-1: the C-truncated human proenzyme
4DPE 1.96 Å, Structure of MMP3 complexed with a platinum-based inhibitor.
4JA1 1.96 Å, Structure of MMP3 complexed with a platinum-based inhibitor
1B8Y 2.0 Å, X-ray structure of human stromelysin catalytic domain complexed with non-peptide…
1CQR 2.0 Å, Crystal structure of the stromelysin catalytic domain at 2.0 a resolution

Browse structure collections

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