2J0T: Catalytic Domain of MMP-1
Crystal Structure of the Catalytic Domain of MMP-1 in Complex with the Inhibitory Domain of TIMP-1. Determined by X-ray diffraction at 2.54 Å resolution. Released 18 Oct 2006.
- Method
- X-ray diffraction
- Resolution
- 2.54 Å
- Organism
- HOMO SAPIENS
- Chains
- 6
- Atoms
- 6,547
- Mol. weight
- 100.55 kDa
- Ligands
- ZN, CA
- Released
- 18 Oct 2006
Explore 2J0T in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
2J0T contains 26 α-helices and 54 β-strands across 6 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: 3 helices, 8 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 113-118 | 6 | 1 |
| α-helix | 127-142 | 16 | |
| β-strand | 148-151 | 4 | 1 |
| β-strand | 159-164 | 6 | 1 |
| β-strand | 180-184 | 5 | 1 |
| β-strand | 195-198 | 4 | 1 |
| β-strand | 204 | 1 | 2 |
| β-strand | 211 | 1 | 2 |
| α-helix | 212-224 | 13 | |
| β-strand | 239 | 1 | 1 |
| α-helix | 250-260 | 11 | |
Chain B: 3 helices, 8 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 113-118 | 6 | 3 |
| α-helix | 127-142 | 16 | |
| β-strand | 148-151 | 4 | 3 |
| β-strand | 159-164 | 6 | 3 |
| β-strand | 180-184 | 5 | 3 |
| β-strand | 195-198 | 4 | 3 |
| β-strand | 204 | 1 | 4 |
| β-strand | 211 | 1 | 4 |
| α-helix | 212-223 | 12 | |
| β-strand | 239 | 1 | 3 |
| α-helix | 250-260 | 11 | |
Chain C: 3 helices, 8 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 113-118 | 6 | 5 |
| α-helix | 127-143 | 17 | |
| β-strand | 148-151 | 4 | 5 |
| β-strand | 159-164 | 6 | 5 |
| β-strand | 180-184 | 5 | 5 |
| β-strand | 195-198 | 4 | 5 |
| β-strand | 204 | 1 | 6 |
| β-strand | 211 | 1 | 6 |
| α-helix | 212-223 | 12 | |
| β-strand | 239 | 1 | 5 |
| α-helix | 250-259 | 10 | |
Chain D: 6 helices, 10 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 | 7 |
| α-helix | 27 | 1 | |
| β-strand | 28-30 | 3 | 8 |
| β-strand | 35-39 | 5 | 8 |
| β-strand | 40-44 | 5 | 7 |
| β-strand | 60-64 | 5 | 8 |
| α-helix | 67-69 | 3 | |
| β-strand | 82-87 | 6 | 7 |
| β-strand | 88-90 | 3 | 8 |
| β-strand | 93-95 | 3 | 8 |
| β-strand | 101-104 | 4 | 7 |
| α-helix | 105-107 | 3 | |
| α-helix | 110-118 | 9 | |
Chain E: 4 helices, 10 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 2-3 | 2 | 3 |
| α-helix | 8-14 | 7 | |
| β-strand | 17-23 | 7 | 9 |
| β-strand | 28 | 1 | 10 |
| β-strand | 35-39 | 5 | 10 |
| β-strand | 40-45 | 6 | 9 |
| 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 | 110-118 | 9 | |
Chain F: 7 helices, 10 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 2-3 | 2 | 5 |
| α-helix | 4-7 | 4 | |
| α-helix | 8-14 | 7 | |
| β-strand | 17-23 | 7 | 11 |
| α-helix | 27 | 1 | |
| β-strand | 28-30 | 3 | 12 |
| β-strand | 35-39 | 5 | 12 |
| β-strand | 40-47 | 8 | 11 |
| β-strand | 60-64 | 5 | 12 |
| α-helix | 67-69 | 3 | |
| β-strand | 82-87 | 6 | 11 |
| β-strand | 88-90 | 3 | 12 |
| β-strand | 93-95 | 3 | 12 |
| β-strand | 102-104 | 3 | 11 |
| α-helix | 105-107 | 3 | |
| α-helix | 113-114 | 2 | |
| α-helix | 115-119 | 5 | |
Molecules and chains
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|
| Interstitial collagenase | A, B, C | protein | 170 | HOMO SAPIENS | P03956 (AlphaFold model) |
| Metalloproteinase inhibitor 1 | D, E, F | protein | 126 | HOMO SAPIENS | P01033 (AlphaFold model) |
Sequence of entity 1 (A, B, C), FASTA
>2J0T_1 INTERSTITIAL COLLAGENASE (chains A, B, C)
MVLTEGNPRWEQTHLTYRIENYTPDLPRADVDHAIEKAFQLWSNVTPLTFTKVSEGQADI
MISFVRGDHRDNSPFDGPGGNLAHAFQPGPGIGGDAHFDEDERWTNNFREYNLHRVAAHE
LGHSLGLSHSTDIGALMYPSYTFSGDVQLAQDDIDGIQAIYGRSQNPVQP
Sequence of entity 2 (D, E, F), FASTA
>2J0T_2 METALLOPROTEINASE INHIBITOR 1 (chains D, E, F)
CTCVPPHPQTAFCNSDLVIRAKFVGTPEVNQTTLYQRYEIKMTKMYKGFQALGDAADIRF
VYTPAMESVCGYFHRSHNRSEEFLIAGKLQDGLLHITTCSFVAPWNSLSLAQRRGFTKTY
TVGCEE
Ligands and cofactors
| ID | Name | Formula | Copies |
|---|
| ZN | Zinc ion | Zn | 6 |
| CA | Calcium ion | Ca | 9 |
Primary citation
Crystal Structure of the Catalytic Domain of Matrix Metalloproteinase-1 in Complex with the Inhibitory Domain of Tissue Inhibitor of Metalloproteinase-1. Iyer, S., Wei, S., Brew, K. et al. J Biol Chem (2007) 282:364. DOI 10.1074/JBC.M607625200 · PubMed
Other PDB entries of the same protein (UniProt P03956 (AlphaFold model), which also has an AlphaFold model), best resolution first:
- 1HFC 1.5 Å, 1.56 Å structure of mature truncated human fibroblast collagenase
- 1CGE 1.9 Å, Crystal structures of recombinant 19-kda human fibroblast collagenase complexed to itself
- 966C 1.9 Å, Crystal structure of fibroblast collagenase-1 complexed to a diphenyl-ether sulphone…
- 1CGF 2.1 Å, Crystal structures of recombinant 19-kda human fibroblast collagenase complexed to itself
- 1SU3 2.2 Å, X-ray structure of human proMMP-1: New insights into collagenase action
- 2TCL 2.2 Å, Structure of the catalytic domain of human fibroblast collagenase complexed with an…
- 3SHI 2.2 Å, Crystal structure of human MMP1 catalytic domain at 2.2 A resolution
- 1CGL 2.4 Å, Structure of the catalytic domain of fibroblast collagenase complexed with an inhibitor
- 2CLT 2.67 Å, Crystal structure of the active form (full-length) of human fibroblast collagenase.
- 4AUO 3.0 Å, Crystal structure of MMP-1(E200A) in complex with a triple-helical collagen peptide
- 1AYK Inhibitor-free catalytic fragment of human fibroblast collagenase, NMR, 30 structures
- 2AYK Inhibitor-free catalytic fragment of human fibroblast collagenase, NMR, minimized…
Browse structure collections
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