SAXSdb — 3ma2

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1. Protein Identity and Related Structures Protein Identity & Related Structures

Matrix metalloproteinase-14

Homo sapiens

State in the Current Structure

Assembly	Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Associated Components	Method and Experimental Conditions	Structure Quality
1	Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain D； UniProt 112–292	Fragment：Residues 112-292	Metalloproteinase inhibitor 1 × 1 （P01033） CA CALCIUM ION × 2 ZN ZINC ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；pH 5.5；292 K；100 mM Bis-Tris pH 5.5, 20% PEG 3350, VAPOR DIFFUSION, HANGING DROP, temperature 292K	Resolution 2.05 Å R-free 0.247
2	Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain A； UniProt 112–292	Fragment：Residues 112-292	Metalloproteinase inhibitor 1 × 1 （P01033） CA CALCIUM ION × 2 ZN ZINC ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；pH 5.5；292 K；100 mM Bis-Tris pH 5.5, 20% PEG 3350, VAPOR DIFFUSION, HANGING DROP, temperature 292K	Resolution 2.05 Å R-free 0.247

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

Other PDB	Difference from Current Entry 3MA2	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1BQQ CRYSTAL STRUCTURE OF THE MT1-MMP--TIMP-2 COMPLEX Deposited 1998-08-18	Different construct Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain M 114–287（174 aa）	Not recorded	CA CALCIUM ION × 2 ZN ZINC ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions pH 5.6；pH 5.60	Resolution 2.75 Å R-free 0.248
1BUV CRYSTAL STRUCTURE OF THE MT1-MMP-TIMP-2 COMPLEX Deposited 1998-09-07	Different construct Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain M 114–287（174 aa）	Not recorded	CA CALCIUM ION × 2 ZN ZINC ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions pH 5.6；pH 5.6	Resolution 2.75 Å R-free 0.248
2MQS Transient Collagen Triple Helix Binding to a Key Metalloproteinase in Invasion and Development: Spin Labels to Structure Deposited 2014-06-26	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain A 316–511（196 aa）	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 5；310 K；Ionic strength (raw mmCIF value) 10；Pressure ambient NMR measurement conditions pH 5；298 K；Ionic strength (raw mmCIF value) 10 mM；Pressure ambient NMR sample composition 300 uM [U-13C; U-15N; U-2H] Hemopexin-like (HPX) of MT1-MMP, 10 mM Sodium acetate, 1 mM EDTA, 1 mM Sodium azide, 93% H2O/7% D2O \| 93% H2O/7% D2O NMR sample composition 0.85 mM THP, 10 mM Sodium acetate, 1 mM EDTA, 1 mM Sodium azide, 93% H2O/7% D2O \| 93% H2O/7% D2O	Resolution not provided
3C7X Hemopexin-like domain of matrix metalloproteinase 14 Deposited 2008-02-08	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 316–511（196 aa） Fragment：UNP residues 316-511	Not recorded	NA SODIUM ION × 1 CL CHLORIDE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6；289 K；2.1M malic acid, 0.1M HCl, 40% acetone, pH 6.0, VAPOR DIFFUSION, SITTING DROP, temperature 289K	Resolution 1.70 Å R-free 0.207
3C7X Hemopexin-like domain of matrix metalloproteinase 14 Deposited 2008-02-08	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 316–511（196 aa） Fragment：UNP residues 316-511	Not recorded	NA SODIUM ION × 2 CL CHLORIDE ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6；289 K；2.1M malic acid, 0.1M HCl, 40% acetone, pH 6.0, VAPOR DIFFUSION, SITTING DROP, temperature 289K	Resolution 1.70 Å R-free 0.207
3C7X Hemopexin-like domain of matrix metalloproteinase 14 Deposited 2008-02-08	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 3 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 316–511（196 aa） Fragment：UNP residues 316-511	Not recorded	NA SODIUM ION × 2 CL CHLORIDE ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6；289 K；2.1M malic acid, 0.1M HCl, 40% acetone, pH 6.0, VAPOR DIFFUSION, SITTING DROP, temperature 289K	Resolution 1.70 Å R-free 0.207
3X23 Radixin complex Deposited 2014-12-09	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain B 563–582（20 aa） Fragment：cytoplasmic tail, UNP residues 563-582	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7；297 K；12% polyethylene glycol 4000, 100mM MOPS (pH 7.0), 100mM NaCl, VAPOR DIFFUSION, SITTING DROP, temperature 297K	Resolution 2.40 Å R-free 0.237
4P3C MT1-MMP:Fab complex (Form I) Deposited 2014-03-06	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 6 PDB declaration: hexameric	Chain M 215–227（13 aa）	Not recorded	CL CHLORIDE ION × 2 EPE 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID × 2 EDO 1,2-ETHANEDIOL × 12 ACT ACETATE ION × 6 MG MAGNESIUM ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；293 K；25% PEG 3350, 0.2M MgCl.hexahydrate, 0.1M Hepes	Resolution 1.94 Å R-free 0.200
4P3D MT1-MMP:Fab complex (Form II) Deposited 2014-03-07	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 6 PDB declaration: hexameric	Chain C 215–227（13 aa） Fragment：MT1-MMP V-B loop Chain M 215–227（13 aa） Fragment：MT1-MMP V-B loop	Not recorded	CL CHLORIDE ION × 2 GOL GLYCEROL × 2 EPE 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID × 2 EDO 1,2-ETHANEDIOL × 3 MG MAGNESIUM ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；293 K；25% PEG 3350, 0.2M MgCl.hexahydrate, 0.1M Hepes	Resolution 1.95 Å R-free 0.210
4QXU Novel Inhibition Mechanism of Membrane Metalloprotease by an Exosite-Swiveling Conformational antibody Deposited 2014-07-22	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain K 218–228（11 aa） Fragment：peptide (unp residues 218-228)	Not recorded	SO4 SULFATE ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6；298 K；0.1M (NH4)2SO4, 0.01M MgCl2 0.05M MES, 16% PEG 8000, VAPOR DIFFUSION, HANGING DROP, temperature 298K	Resolution 2.30 Å R-free 0.293
5H0U Crystal structure of the catalytic domain of membrane type 1 matrix metalloproteinase Deposited 2016-10-07	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 116–285（170 aa）	Not recorded	CA CALCIUM ION × 2 ZN ZINC ION × 3 EPE 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID × 1 GOL GLYCEROL × 8	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；277 K；Ammonium nitrate, PEG3350	Resolution 2.24 Å R-free 0.254
6CLZ MT1-MMP HPX domain with Blade 4 Loop Bound to Nanodiscs Deposited 2018-03-02	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain A 316–511（196 aa） Fragment：residues 316-511	Not recorded	PX4 1,2-DIMYRISTOYL-SN-GLYCERO-3-PHOSPHOCHOLINE × 218 NA SODIUM ION × 1 CL CHLORIDE ION × 1	SOLUTION NMR NMR measurement conditions pH 7.2；303 K；Ionic strength (raw mmCIF value) 300；Pressure 1 NMR sample composition 20 mM Tris-HCl, 300 mM NaCl, 0.02 % sodium azide, 93 % H2O, 7 % [U-100% 2H] D2O, 90 uM 2H, 13C, 15N MT1-MMP hemopexin-like domain, 180 uM MSP1D1, 14.4 mM PX4, 93% H2O/7% D2O \| 93% H2O/7% D2O	Resolution not provided
6CM1 MT1-MMP HPX Domain with Blade 2 Loop Bound to Nanodiscs Deposited 2018-03-02	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain A 316–511（196 aa） Fragment：residues 316-511	Not recorded	PX4 1,2-DIMYRISTOYL-SN-GLYCERO-3-PHOSPHOCHOLINE × 218 NA SODIUM ION × 1 CL CHLORIDE ION × 1	SOLUTION NMR NMR measurement conditions pH 7.2；303 K；Ionic strength (raw mmCIF value) 300；Pressure 1 NMR sample composition 20 mM Tri-HCl, 300 mM NaCl, 0.02 % sodium azide, 93 % H2O, 7 % [U-100% 2H] D2O, 90 uM 2H, 13C, 15N MT1-MMP hemopexin-like domain, 180 uM MSP1D1, 14.4 mM PX4, 93% H2O/7% D2O \| 93% H2O/7% D2O	Resolution not provided

11 other PDB entries and 13 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	MMP14_HUMAN
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–181； UniProt 112–292 Author chain D； PDBConstruct 1–181； UniProt 112–292

Metalloproteinase inhibitor 1

Homo sapiens

UniProt P01033

State in the Current Structure

Assembly	Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Associated Components	Method and Experimental Conditions	Structure Quality
1	Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain C； UniProt 24–148	Fragment：Residues 24-148 Mutation：V27A,P29V,T121L	Matrix metalloproteinase-14 × 1 （P50281） CA CALCIUM ION × 2 ZN ZINC ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；pH 5.5；292 K；100 mM Bis-Tris pH 5.5, 20% PEG 3350, VAPOR DIFFUSION, HANGING DROP, temperature 292K	Resolution 2.05 Å R-free 0.247
2	Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain B； UniProt 24–148	Fragment：Residues 24-148 Mutation：V27A,P29V,T121L	Matrix metalloproteinase-14 × 1 （P50281） CA CALCIUM ION × 2 ZN ZINC ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；pH 5.5；292 K；100 mM Bis-Tris pH 5.5, 20% PEG 3350, VAPOR DIFFUSION, HANGING DROP, temperature 292K	Resolution 2.05 Å R-free 0.247

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

Other PDB	Difference from Current Entry 3MA2	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1D2B THE MMP-INHIBITORY, N-TERMINAL DOMAIN OF HUMAN TISSUE INHIBITOR OF METALLOPROTEINASES-1 (N-TIMP-1), SOLUTION NMR, 29 STRUCTURES Deposited 1999-09-22	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 24–149（126 aa） Fragment：NTR domain, residues 24-149	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 6；293 K；Ionic strength (raw mmCIF value) 0.171；Pressure AMBIENT NMR sample composition 0.5 MM N-TIMP-1 U-15N NMR sample composition 0.9 MM N-TIMP-1 U-15N,13C NMR sample composition 0.7 MM N-TIMP-1 U-15N,13C NMR sample composition 0.4 MM N-TIMP-1 16% 13C NMR sample composition 0.4 MM N-TIMP-1 U-15N,13C	Resolution not provided
1OO9 Orientation in Solution of MMP-3 Catalytic Domain and N-TIMP-1 from Residual Dipolar Couplings Deposited 2003-03-03	Different construct Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain B 24–149（126 aa） Fragment：N-TERMINAL DOMAIN	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 6.6；310 K；Ionic strength (raw mmCIF value) 20mM Tris-d11; 100 mM NaCl; 15 mM CaCl2; 3uM ZnCl2; 1mM Sodium Azide；Pressure ambient NMR measurement conditions pH 6.7；307 K；Ionic strength (raw mmCIF value) 20mM Tris-d11; 125mM NaCl; 15 mM CaCl2; 50uM ZnCl2;1mM Sodium Azide；Pressure ambient NMR sample composition 0.8mM MMP-3 U-15N, 13C; 0.8mM N-TIMP-1; 20mM Tris-d11; 100 mM NaCl; 15 mM CaCl2; 3uM ZnCl2; 1mM Sodium Azide; 93% H2O, 7% D2O \| 93% H2O/7% D2O NMR sample composition 0.5mM MMP-3 U-2H, 15N; 0.5mM N-TIMP-1; 20mM Tris-d11; 100 mM NaCl; 15 mM CaCl2; 3uM ZnCl2; 1mM Sodium Azide; 93% H2O, 7% D2O \| 93% H2O/7% D2O NMR sample composition 0.66mM N-TIMP-1 U-15N, 13C; 0.66mM MMP-3(E202Q); 20mM Tris-d11; 125mM NaCl; 15 mM CaCl2; 50uM ZnCl2; 1mM Sodium Azide; 93% H2O; 7% D2O \| 93% H2O/7% D2O NMR sample composition 0.3mM 98% 2H/15N N-TIMP-1; 0.3mM MMP-3 (E202Q); 20mM Tris-d11; 125mM NaCl; 15 mM CaCl2; 50uM ZnCl2; 1mM Sodium Azide; 93% H2O; 7% D2O \| 93% H2O/7% D2O NMR sample composition 0.3mM 98% 2H/15N N-TIMP-1; 0.3mM (15N-IV, 15N, 13C-L)MMP-3(E202Q); 20mM Tris-d11; 125mM NaCl; 15 mM CaCl2; 50uM ZnCl2; 1mM Sodium Azide; 93% H2O; 7% D2O \| 93% H2O/7% D2O NMR sample composition 0.3mM 98% 2H/15N N-TIMP-1; 0.3mM (15N-IV, 15N, 13C-L)MMP-3(E202Q); 20mM Tris-d11; 125mM NaCl; 15 mM CaCl2; 50uM ZnCl2; 1mM Sodium Azide; 93% H2O; 7% D2O 5% PEG(C12E6)/1-hexanol \| 93% H2O; 7% D2O 5% PEG(C12E6)/1-hexanol	Resolution not provided
1UEA MMP-3/TIMP-1 COMPLEX Deposited 1997-06-06	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain B 24–207（184 aa）	Not recorded	ZN ZINC ION × 2 CA CALCIUM ION × 3	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.80 Å
1UEA MMP-3/TIMP-1 COMPLEX Deposited 1997-06-06	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain D 24–207（184 aa）	Not recorded	ZN ZINC ION × 2 CA CALCIUM ION × 3	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.80 Å
2J0T Crystal Structure of the Catalytic Domain of MMP-1 in Complex with the Inhibitory Domain of TIMP-1 Deposited 2006-08-04	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain D 24–149（126 aa） Fragment：N-TERMINAL INHIBITORY DOMAIN, RESIDUES 24-149	Not recorded	ZN ZINC ION × 2 CA CALCIUM ION × 3	X-RAY DIFFRACTION X-ray crystallization conditions pH 7.5；10% PEG 8000, 8% ETHYLENE GLYCOL, 0.1M HEPES (PH 7.5).	Resolution 2.54 Å R-free 0.275
2J0T Crystal Structure of the Catalytic Domain of MMP-1 in Complex with the Inhibitory Domain of TIMP-1 Deposited 2006-08-04	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain E 24–149（126 aa） Fragment：N-TERMINAL INHIBITORY DOMAIN, RESIDUES 24-149	Not recorded	ZN ZINC ION × 2 CA CALCIUM ION × 3	X-RAY DIFFRACTION X-ray crystallization conditions pH 7.5；10% PEG 8000, 8% ETHYLENE GLYCOL, 0.1M HEPES (PH 7.5).	Resolution 2.54 Å R-free 0.275
2J0T Crystal Structure of the Catalytic Domain of MMP-1 in Complex with the Inhibitory Domain of TIMP-1 Deposited 2006-08-04	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 3 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain F 24–149（126 aa） Fragment：N-TERMINAL INHIBITORY DOMAIN, RESIDUES 24-149	Not recorded	ZN ZINC ION × 2 CA CALCIUM ION × 3	X-RAY DIFFRACTION X-ray crystallization conditions pH 7.5；10% PEG 8000, 8% ETHYLENE GLYCOL, 0.1M HEPES (PH 7.5).	Resolution 2.54 Å R-free 0.275
3V96 Complex of matrix metalloproteinase-10 catalytic domain (MMP-10cd) with tissue inhibitor of metalloproteinases-1 (TIMP-1) Deposited 2011-12-23	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 24–207（184 aa） Fragment：unp residues 24-207	Mutation：N30A	PO4 PHOSPHATE ION × 2 ZN ZINC ION × 2 CA CALCIUM ION × 3	X-RAY DIFFRACTION X-ray crystallization conditions pH 6.5；298 K；0.1 M sodium dihydrogen phosphate solution, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 298K	Resolution 1.90 Å R-free 0.266
6MAV Complex of tissue inhibitor of metalloproteinase-1 (TIMP-1) mutant L34G with matrix metalloproteinase-3 catalytic domain (MMP-3cd) Deposited 2018-08-28	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain B 24–207（184 aa）	Mutation：L34G	CA CALCIUM ION × 3 ZN ZINC ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5.5；298 K；0.1 M Ammonium Acetate 0.1 M Bis-Tris: HCl, pH 5.5, 17 % (w/v) PEG 10,000	Resolution 2.37 Å R-free 0.298
6N9D Complex of tissue inhibitor of metalloproteinases-1 (TIMP-1) mutant (L34G/L133P/L151C/G154A) with matrix metalloproteinase-3 catalytic domain (MMP-3cd) Deposited 2018-12-03	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain B 24–207（184 aa）	Not recorded	CA CALCIUM ION × 3 ZN ZINC ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；298 K；0.2 M Sodium Acetate, 0.1 M Sodium Cacodylate: HCl, pH 6.5 18 % (w/v) PEG 8000	Resolution 2.67 Å R-free 0.258
7S7L Complex of tissue inhibitor of metalloproteinases-1 (TIMP-1) mutant (L34G/M66S/E67Y/L133N/S155L) with matrix metalloproteinase-3 catalytic domain (MMP-3cd) Deposited 2021-09-16	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain B 24–207（184 aa）	Mutation：L34G, M66S, E67Y, L133N, S155L	CA CALCIUM ION × 3 ZN ZINC ION × 2 CL CHLORIDE ION × 1 TRS 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL × 1 SO4 SULFATE ION × 1 GOL GLYCEROL × 1 ACT ACETATE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；310 K；0.2M ammonium sulfate, 0.1M Bis-Tris pH 6.5, 25% w/v PEG 3350 Anatrace-Microlytic Top96 #65	Resolution 2.34 Å R-free 0.239
7S7M Complex of tissue inhibitor of metalloproteinases-1 (TIMP-1) mutant (L34G/M66D/T98G/P131S/Q153N) with matrix metalloproteinase-3 catalytic domain (MMP-3cd) Deposited 2021-09-16	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain B 24–207（184 aa）	Mutation：L34G, M66D, T98G, P131S, Q153N	CA CALCIUM ION × 3 ZN ZINC ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5.5；310 K；0.1 M ammonium acetate, 0.1 M Bis-Tris-HCl, pH 5.5, 17% w/v PEG10000	Resolution 3.00 Å R-free 0.248
9SOP Tissue inhibitor of metalloproteinase-1 (TIMP-1) Deposited 2025-09-15	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 24–203（180 aa）	Not recorded	GOL GLYCEROL × 2 EDO 1,2-ETHANEDIOL × 3 FLC CITRATE ANION × 1 P3G 3,6,9,12,15-PENTAOXAHEPTADECANE × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8.4；293.15 K；0.2 M Lithium Citrate tribasic tetrahydrate, 20% PEG 3350, 15% Glycerol	Resolution 1.95 Å R-free 0.239
9SOP Tissue inhibitor of metalloproteinase-1 (TIMP-1) Deposited 2025-09-15	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 24–203（180 aa）	Not recorded	GOL GLYCEROL × 1 EDO 1,2-ETHANEDIOL × 5 PGE TRIETHYLENE GLYCOL × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8.4；293.15 K；0.2 M Lithium Citrate tribasic tetrahydrate, 20% PEG 3350, 15% Glycerol	Resolution 1.95 Å R-free 0.239
9SOQ Tissue inhibitor of Metalloproteinase 1 (TIMP-1) Deposited 2025-09-15	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 24–207（184 aa）	Not recorded	FLC CITRATE ANION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 5.6；293.15 K；0.2 Ammonium Sulphate, 0.1 M tri-sodium citrate, 25% PEG4000	Resolution 2.30 Å R-free 0.262
9SOQ Tissue inhibitor of Metalloproteinase 1 (TIMP-1) Deposited 2025-09-15	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 24–207（184 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 5.6；293.15 K；0.2 Ammonium Sulphate, 0.1 M tri-sodium citrate, 25% PEG4000	Resolution 2.30 Å R-free 0.262
9SOS Tissue Inhibitor of Matrix Metalloproteinase-1 (TIMP-1) Deposited 2025-09-15	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 24–207（184 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8.4；293.15 K；0.2 M Lithium Citrate tribasic tetrahydrate, 20% PEG3350	Resolution 2.00 Å R-free 0.255

12 other PDB entries and 17 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	TIMP1_HUMAN
Isoform	—
PDB entities	2
Chains and sequence ranges	Author chain B； PDBConstruct 1–125； UniProt 24–148 Author chain C； PDBConstruct 1–125； UniProt 24–148

The page prioritizes protein identity, the current assembly, associated components, oligomeric state and cross-PDB links. Chain mapping and sequence ranges are retained as data evidence. Internal IDs, import timestamps and assembly operation expressions are maintenance fields and are not shown here.

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2. Structure Basics 2. Structure Basics

Entry ID entry_id	3ma2
Deposition date deposition_date	2010-03-23
Structure title title	Complex membrane type-1 matrix metalloproteinase (MT1-MMP) with tissue inhibitor of metalloproteinase-1 (TIMP-1)
Keywords keywords	;Protein - protein complex, Cleavage on pair of basic residues, Disulfide bond, Membrane, Metal-binding, Metalloprotease, Protease, Transmembrane, Zymogen, Erythrocyte maturation, Glycoprotein, Metalloenzyme inhibitor, Metalloprotease inhibitor, Secreted, HYDROLASE-HYDROLASE INHIBITOR complex ;; HYDROLASE/HYDROLASE INHIBITOR
Experimental Method method	X-RAY DIFFRACTION

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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier	27.29 Å
Radius of gyration Rg (electron density) rg_electron	26.50 Å
Forward intensity I(0) i0	70028100.00
Molecular weight molecular_weight	64858.0 kDa
Excluded volume excluded_volume	80610 Å³
Envelope volume envelope_volume	99408 Å³
Hydration-shell volume shell_volume	31322 Å³
Envelope diameter envelope_diameter	93.7 Å
Shell Rg shell_rg	33.86 Å
Envelope Rg envelope_rg	26.35 Å
Shape Rg shape_rg	26.51 Å
Total Rg total_rg	27.23 Å
Total atoms total_atoms	4564
Residues n_residues	575
Spherical-harmonic order n_harmonics	20
q range q_range	— – 0.5000 Å⁻¹
Data points n_points	101
Shell type shell_type	directional
Solvent electron density solvent_density	0.3340 e/Å³
Shell contrast contrast_shell	0.0300 e/Å³
CRYSOL version crysol_version	4.1.3

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4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax	90.7 Å
Rg (real space) rg_real	27.23 Å
Rg uncertainty (real space) rg_real_error	0.77 Å
I(0) (real space) i0_real	7.0030e+07
I(0) uncertainty (real space) i0_real_error	1.0620e+06
Rg (reciprocal space) rg_reciprocal	27.25 Å
I(0) (reciprocal space) i0_reciprocal	70030000.0000
Solution quality estimate total_estimate	0.8907
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	31.3 Å
Skewness Skewness skewness	0.270
Kurtosis Kurtosis kurtosis	-0.401
Angular range angular_range	— – 0.2900 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	15760000.0000
Real-space data points n_real_points	59
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.870; Stabil: 0.998; Sysdev: 1.000; Positv: 1.000; Valcen: 0.997; Smooth: 0.974

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (5)

Entity 1 Entity 1 polymer

Description description	Matrix metalloproteinase-14
Molecular weight formula_weight	20561.7 kDa
EC 编号 ec_number	3.4.24.80
Source method src_method	man
Copy count entity_count	2

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	D,A
Atom count atom_count	4709

YAIQGLKWQHNEITFCIQNYTPKVGEYATYEAIRKAFRVWESATPLRFREVPYAYIREGHEKQADIMIFFAEGFHGDSTPFDGEGGFLAHAYFPGPNIGGDTHFDSAEPWTVRNEDLNGNDIFLVAVHELGHALGLEHSSDPSAIMAPFYQWMDTENFVLPDDDRRGIQQLYGGESGFPTK

来源 Source

来源生物 organism	Homo sapiens
通用名 common_name	human
NCBI Class编号 ncbi_taxonomy_id	9606
宿主生物 host_organism	Escherichia coli

Entity 2 Entity 2 polymer

Description description	Metalloproteinase inhibitor 1
Molecular weight formula_weight	14126.2 kDa
Mutation mutation	V27A,P29V,T121L
Source method src_method	man
Copy count entity_count	2

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	B,C

CTCAPVHPQTAFCNSDLVIRAKFVGTPEVNQTTLYQRYEIKMTKMYKGFQALGDAADIRFVYTPAMESVCGYFHRSHNRSEEFLIAGKLQDGLLHITLCSFVAPWNSLSLAQRRGFTKTYTVGCE

来源 Source

来源生物 organism	Homo sapiens
通用名 common_name	human
NCBI Class编号 ncbi_taxonomy_id	9606
宿主生物 host_organism	Escherichia coli

Entity 3 Entity 3 non-polymer

Description description	CALCIUM ION
Molecular weight formula_weight	40.1 kDa
Source method src_method	syn
Copy count entity_count	4

Entity 4 Entity 4 non-polymer

Description description	ZINC ION
Molecular weight formula_weight	65.4 kDa
Source method src_method	syn
Copy count entity_count	4

Entity 5 Entity 5 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	145

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7. Fold Classification (SCOP + CATH) 8 domains

SCOP 2.08 (4 domains)

Domain ID domain_id	d3ma2a_
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.92 — Zincin-like
Superfamily Superfamily superfamily	d.92.1 — Metalloproteases ('zincins'), catalytic domain
Family Family family	d.92.1.11 — Matrix metalloproteases, catalytic domain

Domain ID domain_id	d3ma2b_
Class class	b — All beta proteins
Fold Fold fold	b.40 — OB-fold
Superfamily Superfamily superfamily	b.40.3 — TIMP-like
Family Family family	b.40.3.1 — Tissue inhibitor of metalloproteinases, TIMP

Domain ID domain_id	d3ma2c_
Class class	b — All beta proteins
Fold Fold fold	b.40 — OB-fold
Superfamily Superfamily superfamily	b.40.3 — TIMP-like
Family Family family	b.40.3.1 — Tissue inhibitor of metalloproteinases, TIMP

Domain ID domain_id	d3ma2d_
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.92 — Zincin-like
Superfamily Superfamily superfamily	d.92.1 — Metalloproteases ('zincins'), catalytic domain
Family Family family	d.92.1.11 — Matrix metalloproteases, catalytic domain

CATH v4.4 (4 domains)

Domain ID domain_id	3ma2A00
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	390 — Collagenase (Catalytic Domain)
Homologous superfamily homologous superfamily	10 — Collagenase (Catalytic Domain)

Domain ID domain_id	3ma2B00
Class class	2 — Mainly Beta
Architecture architecture	40 — Beta Barrel
Topology topology	50 — OB fold (Dihydrolipoamide Acetyltransferase, E2P)
Homologous superfamily homologous superfamily	120 —

Domain ID domain_id	3ma2C00
Class class	2 — Mainly Beta
Architecture architecture	40 — Beta Barrel
Topology topology	50 — OB fold (Dihydrolipoamide Acetyltransferase, E2P)
Homologous superfamily homologous superfamily	120 —

Domain ID domain_id	3ma2D00
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	390 — Collagenase (Catalytic Domain)
Homologous superfamily homologous superfamily	10 — Collagenase (Catalytic Domain)

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8. Citations (1)

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Unit-cell length a length_a	59.690 Å
Unit-cell length b length_b	63.649 Å
Unit-cell length c length_c	87.158 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	105.86 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	4

Space group space_group	P 1 21 1
Space-group number int_tables_number	4
Crystal system crystal_system	—

Resolution resolution	2.050 Å
Low-resolution limit resolution_low	50.000 Å
R factor r_factor	0.1991
R_work r_work	0.1964
R_free r_free	0.2471

fit	/app/data/saxs_computation/ma/3ma2/3ma2.fit
pddf	/app/data/pr_computation/ma/3ma2/3ma2.pr.out
profile	/app/data/saxs_computation/ma/3ma2/3ma2.dat

Complex membrane type-1 matrix metalloproteinase (MT1-MMP) with tissue inhibitor of metalloproteinase-1 (TIMP-1)

1. Protein Identity and Related Structures Protein Identity & Related Structures

Matrix metalloproteinase-14

State in the Current Structure

Other States of the Same Protein in the Database

Metalloproteinase inhibitor 1

State in the Current Structure

Other States of the Same Protein in the Database

SAXS scattering curve SAXS Profile

P(r) Distance Distribution P(r) Distribution

2. Structure Basics 2. Structure Basics

3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

5. Crystallography and Experiment 5. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

Refinement Refinement

Diffraction experiment Diffraction

6. Entities and Polymers Entities & Polymers (5)

Entity 1 Entity 1 polymer

Polymer Polymer

来源 Source

Entity 2 Entity 2 polymer

Polymer Polymer

来源 Source

Entity 3 Entity 3 non-polymer

Entity 4 Entity 4 non-polymer

Entity 5 Entity 5 water

7. Fold Classification (SCOP + CATH) 8 domains

SCOP 2.08 (4 domains)

CATH v4.4 (4 domains)

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)