SAXSdb — 3c7x

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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 monomer Monomer Protein × 1 PDB declaration: monomeric（1） Consistent with protein copy count	Chain A； UniProt 316–511	Fragment：UNP residues 316-511	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
2	Protein homooligomer Homooligomer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain A； UniProt 316–511	Fragment：UNP residues 316-511	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
3	Protein homooligomer Homooligomer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain A； UniProt 316–511	Fragment：UNP residues 316-511	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

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 3C7X	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 oligomeric state Different ligand/ion 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 oligomeric state Different ligand/ion 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
3MA2 Complex membrane type-1 matrix metalloproteinase (MT1-MMP) with tissue inhibitor of metalloproteinase-1 (TIMP-1) Deposited 2010-03-23	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain D 112–292（181 aa） Fragment：Residues 112-292	Not recorded	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
3MA2 Complex membrane type-1 matrix metalloproteinase (MT1-MMP) with tissue inhibitor of metalloproteinase-1 (TIMP-1) Deposited 2010-03-23	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 112–292（181 aa） Fragment：Residues 112-292	Not recorded	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
3X23 Radixin complex Deposited 2014-12-09	Different construct Different oligomeric state 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 oligomeric state 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 12 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 1–196； UniProt 316–511

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	3c7x
Deposition date deposition_date	2008-02-08
Structure title title	Hemopexin-like domain of matrix metalloproteinase 14
Keywords keywords	;membrane protein interaction, pro-MMP-2, TIMP-2, metastasis, Cleavage on pair of basic residues, Hydrolase, Metal-binding, Metalloprotease, Protease, Transmembrane, Zymogen ;; HYDROLASE
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	17.50 Å
Radius of gyration Rg (electron density) rg_electron	16.10 Å
Forward intensity I(0) i0	9309690.00
Molecular weight molecular_weight	23164.0 kDa
Excluded volume excluded_volume	29146 Å³
Envelope volume envelope_volume	32095 Å³
Hydration-shell volume shell_volume	16428 Å³
Envelope diameter envelope_diameter	55.0 Å
Shell Rg shell_rg	22.48 Å
Envelope Rg envelope_rg	16.42 Å
Shape Rg shape_rg	16.05 Å
Total Rg total_rg	17.31 Å
Total atoms total_atoms	1639
Residues n_residues	196
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	53.6 Å
Rg (real space) rg_real	17.37 Å
Rg uncertainty (real space) rg_real_error	0.25 Å
I(0) (real space) i0_real	9.3100e+06
I(0) uncertainty (real space) i0_real_error	1.0710e+05
Rg (reciprocal space) rg_reciprocal	17.39 Å
I(0) (reciprocal space) i0_reciprocal	9310000.0000
Solution quality estimate total_estimate	0.8219
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	21.5 Å
Skewness Skewness skewness	0.123
Kurtosis Kurtosis kurtosis	-0.412
Angular range angular_range	— – 0.4550 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	2224000.0000
Real-space data points n_real_points	76
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.900; Stabil: 0.998; Sysdev: 1.000; Positv: 1.000; Valcen: 0.986; Smooth: 0.000

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (4)

Entity 1 Entity 1 polymer

Description description	Matrix metalloproteinase-14
Molecular weight formula_weight	23131.3 kDa
EC 编号 ec_number	3.4.24.80
Source method src_method	man
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A
Atom count atom_count	1874

PNICDGNFDTVAMLRGEMFVFKERWFWRVRNNQVMDGYPMPIGQFWRGLPASINTAYERKDGKFVFFKGDKHWVFDEASLEPGYPKHIKELGRGLPTDKIDAALFWMPNGKTYFFRGNKYYRFNEELRAVDSEYPKNIKVWEGIPESPRGSFMGSDEVFTYFYKGNKYWKFNNQKLKVEPGYPKSALRDWMGCPSG

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	Homo sapiens

Entity 2 Entity 2 non-polymer

Description description	SODIUM ION
Molecular weight formula_weight	23.0 kDa
Source method src_method	syn
Copy count entity_count	1

Entity 3 Entity 3 non-polymer

Description description	CHLORIDE ION
Molecular weight formula_weight	35.5 kDa
Source method src_method	syn
Copy count entity_count	1

Entity 4 Entity 4 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	235

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7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_id	d3c7xa_
Class class	b — All beta proteins
Fold Fold fold	b.66 — 4-bladed beta-propeller
Superfamily Superfamily superfamily	b.66.1 — Hemopexin-like domain
Family Family family	b.66.1.0 — automated matches

CATH v4.4 (1 domains)

Domain ID domain_id	3c7xA00
Class class	2 — Mainly Beta
Architecture architecture	110 — 4 Propeller
Topology topology	10 — Hemopexin
Homologous superfamily homologous superfamily	10 — Hemopexin-like domain

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8. Citations (1)

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Unit-cell length a length_a	77.210 Å
Unit-cell length b length_b	77.210 Å
Unit-cell length c length_c	66.819 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	90.00 °
Unit-cell angle γ angle_gamma	120.00 °
Molecules per unit cell Z z_pdb	6

Space group space_group	P 31 2 1
Space-group number int_tables_number	152
Crystal system crystal_system	—

Resolution resolution	1.700 Å
Low-resolution limit resolution_low	19.290 Å
R factor r_factor	0.1850
R_work r_work	0.1850
R_free r_free	0.2070

fit	/app/data/saxs_computation/c7/3c7x/3c7x.fit
pddf	/app/data/pr_computation/c7/3c7x/3c7x.pr.out
profile	/app/data/saxs_computation/c7/3c7x/3c7x.dat

Hemopexin-like domain of matrix metalloproteinase 14

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

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