1UEA: Mmp-3/TIMP-1 complex

Mmp-3/TIMP-1 complex. Determined by X-ray diffraction at 2.8 Å resolution. Released 14 Oct 1998.

Method: X-ray diffraction
Resolution: 2.8 Å
Organism: Homo sapiens
Chains: 4
Atoms: 6,039
Mol. weight: 80.82 kDa
Ligands: CA, ZN
Released: 14 Oct 1998

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

Secondary structure: helices and β-sheets

1UEA contains 25 α-helices and 44 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, 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: 8 helices, 14 β-strands

Element	Residues	Length	Sheet
β-strand	2-3	2	1
α-helix	5-7	3
α-helix	8-14	7
β-strand	17-23	7	3
β-strand	28-29	2	4
β-strand	35-39	5	4
β-strand	40-47	8	3
β-strand	60-64	5	4
α-helix	67-69	3
β-strand	83-87	5	3
β-strand	88-90	3	4
β-strand	93-95	3	4
β-strand	102-104	3	3
α-helix	105-107	3
α-helix	110-114	5
α-helix	115-119	5
α-helix	120-124	5
β-strand	128-131	4	5
β-strand	144-147	4	5
α-helix	159-163	5
β-strand	164-170	7	6
β-strand	173-178	6	6

Chain C: 3 helices, 8 β-strands

Element	Residues	Length	Sheet
β-strand	96-101	6	7
α-helix	110-125	16
β-strand	131-134	4	7
β-strand	142-147	6	7
β-strand	163-167	5	7
β-strand	178-181	4	7
β-strand	186-187	2	8
β-strand	193-194	2	8
α-helix	195-206	12
β-strand	222	1	7
α-helix	236-246	11

Chain D: 10 helices, 14 β-strands

Element	Residues	Length	Sheet
β-strand	2-3	2	7
α-helix	4-7	4
α-helix	8-14	7
β-strand	17-23	7	9
β-strand	28-29	2	10
β-strand	35-39	5	10
β-strand	40-47	8	9
α-helix	49-51	3
β-strand	60-64	5	10
α-helix	67-69	3
β-strand	82-87	6	9
β-strand	88-90	3	10
β-strand	93-95	3	10
β-strand	102-104	3	9
α-helix	105-107	3
α-helix	110-114	5
α-helix	115-119	5
α-helix	121-124	4
β-strand	128-131	4	11
α-helix	132	1
β-strand	144-147	4	11
α-helix	159-163	5
β-strand	164-170	7	12
β-strand	173-178	6	12

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Matrix metalloproteinase-3	A, C	protein	173	Homo sapiens	P08254 (AlphaFold model)
Tissue inhibitor of metalloproteinase-1	B, D	protein	184	Homo sapiens	P01033 (AlphaFold model)

Sequence of entity 1 (A, C), FASTA

>1UEA_1 MATRIX METALLOPROTEINASE-3 (chains A, C)
FRTFPGIPKWRKTHLTYRIVNYTPDLPKDAVDSAVEKALKVWEEVTPLTFSRLYEGEADI
MISFAVREHGDFYPFDGPGNVLAHAYAPGPGINGDAHFDDDEQWTKDTTGTNLFLVAAHE
IGHSLGLFHSANTEALMYPLYHSLTDLTRFRLSQDDINGIQSLYGPPPDSPET

Sequence of entity 2 (B, D), FASTA

>1UEA_2 TISSUE INHIBITOR OF METALLOPROTEINASE-1 (chains B, D)
CTCVPPHPQTAFCNSDLVIRAKFVGTPEVAQTTLYQRYEIKMTKMYKGFQALGDAADIRF
VYTPAMESVCGYFHRSHARSEEFLIAGKLQDGLLHITTCSFVAPWNSLSLAQRRGFTKTY
TVGCEECTVFPCLSIPCKLQSGTHCLWTDQLLQGSEKGFQSRHLACLPREPGLCTWQSLR
SQIA

Ligands and cofactors

ID	Name	Formula	Copies
CA	Calcium ion	Ca	6
ZN	Zinc ion	Zn	4

Primary citation

Mechanism of inhibition of the human matrix metalloproteinase stromelysin-1 by TIMP-1. Gomis-Ruth, F.X., Maskos, K., Betz, M. et al. Nature (1997) 389:77-81. DOI 10.1038/37995 · 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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