1OO9: Stromelysin-1

Orientation in Solution of MMP-3 Catalytic Domain and N-TIMP-1 from Residual Dipolar Couplings. Determined by solution NMR. Released 29 Jul 2003.

Method: Solution NMR
Organism: Homo sapiens
Chains: 2
Atoms: 2,337
Mol. weight: 33.16 kDa
Released: 29 Jul 2003

Explore 1OO9 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1OO9 contains 11 α-helices and 18 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: 4 helices, 8 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	163-167	5	1
β-strand	178-181	4	1
β-strand	186-187	2	2
β-strand	193-194	2	2
α-helix	195-206	12
β-strand	222	1	1
α-helix	229-231	3
α-helix	236-246	11

Chain B: 7 helices, 10 β-strands

Element	Residues	Length	Sheet
β-strand	302-303	2	1
α-helix	305-307	3
α-helix	308-314	7
β-strand	317-323	7	3
β-strand	328-329	2	4
β-strand	335-339	5	4
β-strand	340-347	8	3
β-strand	360-364	5	4
α-helix	367-369	3
β-strand	383-387	5	3
β-strand	388-390	3	4
β-strand	393-395	3	4
β-strand	402-404	3	3
α-helix	405-407	3
α-helix	410-414	5
α-helix	415-419	5
α-helix	420-424	5

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Stromelysin-1	A	protein	168	Homo sapiens	P08254 (AlphaFold model)
Metalloproteinase inhibitor 1	B	protein	126	Homo sapiens	P01033 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>1OO9_1 Stromelysin-1 (chains A)
FRTFPGIPKWRKTHLTYRIVNYTPDLPKDAVDSAVEKALKVWEEVTPLTFSRLYEGEADI
MISFAVREHGDFYPFDGPGNVLAHAYAPGPGINGDAHFDDDEQWTKDTTGTNLFLVAAHE
IGHSLGLFHSANTEALMYPLYHSLTDLTRFRLSQDDINGIQSLYGPPP

Sequence of entity 2 (B), FASTA

>1OO9_2 Metalloproteinase inhibitor 1 (chains B)
CTCVPPHPQTAFCNSDLVIRAKFVGTPEVNQTTLYQRYEIKMTKMYKGFQALGDAADIRF
VYTPAMESVCGYFHRSHNRSEEFLIAGKLQDGLLHITTCSFVAPWNSLSLAQRRGFTKTY
TVGCEE

Primary citation

Global Orientation of Bound MMP-3 and N-TIMP-1 in Solution via Residual Dipolar Couplings. Arumugam, S., Van Doren, S.R. Biochemistry (2003) 42:7950-7958. DOI 10.1021/bi034545s · 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…

Browse structure collections

About this viewer

MolViewer shows 1OO9 directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.