1QIA: Stromelysin catalytic domain

Crystal structure of stromelysin catalytic domain. Determined by X-ray diffraction at 2.0 Å resolution. Released 11 Feb 2003.

Method: X-ray diffraction
Resolution: 2.0 Å
Organism: Homo sapiens
Chains: 4
Atoms: 5,764
Mol. weight: 73.73 kDa
Ligands: CA, ZN
Released: 11 Feb 2003

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

Secondary structure: helices and β-sheets

1QIA contains 16 α-helices and 28 β-strands across 4 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	96-101	6	1
α-helix	110-125	16
β-strand	131-134	4	1
β-strand	142-147	6	1
β-strand	165-167	3	1
β-strand	178-181	4	1
β-strand	187	1	2
β-strand	194	1	2
α-helix	195-206	12
α-helix	229-231	3
α-helix	236-246	11

Chains B and C: 4 helices, 7 β-strands

Element	Residues	Length	Sheet
β-strand	96-101	6	3
α-helix	110-125	16
β-strand	131-134	4	3
β-strand	142-147	6	3
β-strand	165-167	3	3
β-strand	178-181	4	3
β-strand	186-187	2	4
β-strand	193-194	2	4
α-helix	195-206	12
α-helix	229-231	3
α-helix	236-246	11

Chain D: 4 helices, 7 β-strands

Element	Residues	Length	Sheet
β-strand	96-101	6	7
α-helix	110-127	18
β-strand	131-134	4	7
β-strand	142-147	6	7
β-strand	165-167	3	7
β-strand	178-181	4	7
β-strand	186-187	2	8
β-strand	193-194	2	8
α-helix	195-206	12
α-helix	229-231	3
α-helix	236-246	11

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Stromelysin-1	A, B, C, D	protein	162	Homo sapiens	P08254 (AlphaFold model)

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

>1QIA_1 STROMELYSIN-1 (chains A, B, C, D)
IPKWRKTHLTYRIVNYTPDLPKDAVDSAVEKALKVWEEVTPLTFSRLYEGEADIMISFAV
REHGDFYPFDGPGNVLAHAYAPGPGINGDAHFDDDEQWTKDTTGTNLFLVAAHEIGHSLG
LFHSANTEALMYPLYHSLTDLTRFRLSQDDINGIQSLYGPPP

Ligands and cofactors

ID	Name	Formula	Copies
CA	Calcium ion	Ca	12
ZN	Zinc ion	Zn	8

Primary citation

X-ray structure of human stromelysin catalytic domain complexed with nonpeptide inhibitors: implications for inhibitor selectivity. Pavlovsky, A.G., Williams, M.G., Ye, Q.-Z. et al. Protein Sci (1999) 8:1455-1462. 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…
1C3I 1.83 Å, Human stromelysin-1 catalytic domain complexed with ro-26-2812
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…

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