1gxd

proMMP-2/TIMP-2 complex

Method: X-RAY DIFFRACTION D_max: 221.4 Å Quality: REASONABLE

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

72 KDA TYPE IV COLLAGENASE

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 A； UniProt 30–660	Mutation：YES	METALLOPROTEINASE INHIBITOR 2 × 1 （P16035） SO4 SULFATE ION × 1 ZN ZINC ION × 2 CA CALCIUM ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions：pH 8.5；pH 8.50	Resolution 3.10 Å R-free 0.333
2	Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain B； UniProt 30–660	Mutation：YES	METALLOPROTEINASE INHIBITOR 2 × 1 （P16035） SO4 SULFATE ION × 1 ZN ZINC ION × 2 CA CALCIUM ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions：pH 8.5；pH 8.50	Resolution 3.10 Å R-free 0.333

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 1GXD	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1CK7 GELATINASE A (FULL-LENGTH) Deposited 1999-04-28	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 30–660（631 aa） Fragment：FULL-LENGTH	Mutation：E404A	ZN ZINC ION × 2 CA CALCIUM ION × 3 CL CHLORIDE ION × 1 NA SODIUM ION × 1 SO4 SULFATE ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions pH 7.8；pH 7.8	Resolution 2.80 Å R-free 0.327
1CXW THE SECOND TYPE II MODULE FROM HUMAN MATRIX METALLOPROTEINASE 2 Deposited 1999-08-31	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 278–336（59 aa） Fragment：THE SECOND TYPE II MODULE	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 5.2；298 K；Ionic strength (raw mmCIF value) 0；Pressure 1 NMR measurement conditions pH 5.1；298 K；Ionic strength (raw mmCIF value) 0；Pressure 1 NMR sample composition 1.3MM COL-2 NA; 90% H2O, 10% D2O NMR sample composition 1.3MM COL-2 NA; D2O NMR sample composition 1MM COL-2 U-15N; 90% H2O, 10% D2O NMR sample composition 4MM COL-2 U-15N; 90% H2O, 10% D2O	Resolution not provided
1EAK Catalytic domain of proMMP-2 E404Q mutant Deposited 2001-07-12	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain A 32–452（421 aa） Fragment：CATALYTIC DOMAIN RESIDUES 32-452 Chain C 32–452（421 aa） Fragment：CATALYTIC DOMAIN RESIDUES 32-452	Mutation：YES Mutation：YES	SO4 SULFATE ION × 3 ZN ZINC ION × 4 CA CALCIUM ION × 4	X-RAY DIFFRACTION X-ray crystallization conditions pH 8.5；PH 8.50	Resolution 2.66 Å R-free 0.303
1EAK Catalytic domain of proMMP-2 E404Q mutant Deposited 2001-07-12	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain B 32–452（421 aa） Fragment：CATALYTIC DOMAIN RESIDUES 32-452 Chain D 32–452（421 aa） Fragment：CATALYTIC DOMAIN RESIDUES 32-452	Mutation：YES Mutation：YES	SO4 SULFATE ION × 3 ZN ZINC ION × 4 CA CALCIUM ION × 4	X-RAY DIFFRACTION X-ray crystallization conditions pH 8.5；PH 8.50	Resolution 2.66 Å R-free 0.303
1GEN C-TERMINAL DOMAIN OF GELATINASE A Deposited 1995-07-19	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 443–660（218 aa） Fragment：C-TERMINAL DOMAIN	Not recorded	ZN ZINC ION × 1 CA CALCIUM ION × 1 CL CHLORIDE ION × 1 NA SODIUM ION × 1	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.15 Å R-free 0.260
1HOV SOLUTION STRUCTURE OF A CATALYTIC DOMAIN OF MMP-2 COMPLEXED WITH SC-74020 Deposited 2000-12-11	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 110–256（147 aa） Fragment：CATALYTIC DOMAIN	Not recorded	ZN ZINC ION × 2 CA CALCIUM ION × 2 I52 N-{4-[(1-HYDROXYCARBAMOYL-2-METHYL-PROPYL)-(2-MORPHOLIN-4-YL-ETHYL)-SULFAMOYL]-4-PENTYL-BENZAMIDE × 1	SOLUTION NMR NMR measurement conditions pH 7.4；303 K；Ionic strength (raw mmCIF value) 50；Pressure 1 NMR sample composition 0.3-0.4mM U-15N, 13C MMP-2C: unlabeled SC-74020 in 20mM TRIS-d11-HCl, 5mM CaCl2, 10uM ZnCl2, 20uM unlabeled SC-74020 \| 90% H2O/10% D2O	Resolution not provided
1J7M The Third Fibronectin Type II Module from Human Matrix Metalloproteinase 2 Deposited 2001-05-17	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 337–394（58 aa） Fragment：third fibronectin type II module	Mutation：E11G	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 5.4；298 K；Ionic strength (raw mmCIF value) 0；Pressure ambient NMR sample composition 0.5mM col-3 NA; 90% H2O, 10% D2O \| 90% H2O/10% D2O NMR sample composition 0.5mM col-3 NA; D2O \| D2O NMR sample composition 1mM col-3 U-15n; 90% H2O, 10% D2O \| 90% H2O/10% D2O	Resolution not provided
1KS0 The First Fibronectin Type II Module from Human Matrix Metalloproteinase 2 Deposited 2002-01-10	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 223–282（60 aa） Fragment：First Fibronectin Type II Module	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 7.3；298 K；Ionic strength (raw mmCIF value) 0；Pressure ambient NMR measurement conditions pH 6；298 K；Ionic strength (raw mmCIF value) 0；Pressure ambient NMR sample composition 0.5mM col-1; 90% H2O, 10% d6-acetone \| 90% H2O, 10% d6-acetone NMR sample composition 0.5mM col-1; 90% D2O, 10% d6-acetone \| 90% D2O, 10% d6-acetone NMR sample composition 0.7mM col-1 15N; 90% H2O, 10% d6-acetone \| 90% H2O, 10% d6-acetone	Resolution not provided
1QIB CRYSTAL STRUCTURE OF GELATINASE A CATALYTIC DOMAIN Deposited 1999-06-11	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 115–213（99 aa） Fragment：CATALYTIC DOMAIN RESIDUES 88-250 WITH THE FIBRONECTIN DOMAIN DELETED Chain A 394–449（56 aa） Fragment：CATALYTIC DOMAIN RESIDUES 88-250 WITH THE FIBRONECTIN DOMAIN DELETED	Not recorded	ZN ZINC ION × 2 CA CALCIUM ION × 3	X-RAY DIFFRACTION X-ray crystallization conditions pH 6；pH 6.0	Resolution 2.80 Å R-free 0.244
1RTG C-TERMINAL DOMAIN (HAEMOPEXIN-LIKE DOMAIN) OF HUMAN MATRIX METALLOPROTEINASE-2 Deposited 1995-12-21	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 451–660（210 aa） Fragment：C-TERMINAL RESIDUES 451 - 660, HAEMOPEXIN-LIKE DOMAIN	Not recorded	CL CHLORIDE ION × 1 CA CALCIUM ION × 2	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.60 Å
3AYU Crystal structure of MMP-2 active site mutant in complex with APP-drived decapeptide inhibitor Deposited 2011-05-17	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 110–219（110 aa） Fragment：UNP residues 110-219 and 394-450 Chain A 394–450（57 aa） Fragment：UNP residues 110-219 and 394-450	Mutation：E108K, Q110V, E121A Mutation：E108K, Q110V, E121A	ZN ZINC ION × 2 CA CALCIUM ION × 3	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.00 Å R-free 0.205

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

View Construct and Data Evidence

UniProt name	MM02_HUMAN
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–631； UniProt 30–660 Author chain B； PDBConstruct 1–631； UniProt 30–660

METALLOPROTEINASE INHIBITOR 2

HOMO SAPIENS

UniProt P16035

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 27–220	Not recorded	72 KDA TYPE IV COLLAGENASE × 1 （P08253） SO4 SULFATE ION × 1 ZN ZINC ION × 2 CA CALCIUM ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions：pH 8.5；pH 8.50	Resolution 3.10 Å R-free 0.333
2	Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain D； UniProt 27–220	Not recorded	72 KDA TYPE IV COLLAGENASE × 1 （P08253） SO4 SULFATE ION × 1 ZN ZINC ION × 2 CA CALCIUM ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions：pH 8.5；pH 8.50	Resolution 3.10 Å R-free 0.333

Other States of the Same Protein in the Database

Other PDB	Difference from Current Entry 1GXD	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1BR9 HUMAN TISSUE INHIBITOR OF METALLOPROTEINASE-2 Deposited 1998-08-28	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 27–220（194 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions pH 8；pH 8.0	Resolution 2.10 Å R-free 0.271
2TMP N-TERMINAL DOMAIN OF TISSUE INHIBITOR OF METALLOPROTEINASE-2 (N-TIMP-2), NMR, 49 STRUCTURES Deposited 1998-05-26	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 27–153（127 aa） Fragment：N-TERMINAL DOMAIN, RESIDUES 1-127	Mutation：A21T	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 6.7；308 K；Ionic strength (raw mmCIF value) 125 mM；Pressure 1 NMR sample composition AQUEOUS	Resolution not provided
4ILW Complex of matrix metalloproteinase-10 catalytic domain (MMP-10cd) with tissue inhibitor of metalloproteinases-2 (TIMP-2) Deposited 2013-01-01	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 27–220（194 aa） Fragment：Tissue inhibitor of metalloproteinases-2	Not recorded	ZN ZINC ION × 2 CA CALCIUM ION × 3	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION；pH 7.5；298 K；0.1 M HEPES pH 7.5, 25 % (w/v) PEG 2000 MME, VAPOR DIFFUSION, temperature 298K	Resolution 2.10 Å R-free 0.263
4ILW Complex of matrix metalloproteinase-10 catalytic domain (MMP-10cd) with tissue inhibitor of metalloproteinases-2 (TIMP-2) Deposited 2013-01-01	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain B 27–220（194 aa） Fragment：Tissue inhibitor of metalloproteinases-2	Not recorded	ZN ZINC ION × 2 CA CALCIUM ION × 3	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION；pH 7.5；298 K；0.1 M HEPES pH 7.5, 25 % (w/v) PEG 2000 MME, VAPOR DIFFUSION, temperature 298K	Resolution 2.10 Å R-free 0.263

3 other PDB entries and 4 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	TIM2_HUMAN
Isoform	—
PDB entities	2
Chains and sequence ranges	Author chain C； PDBConstruct 1–194； UniProt 27–220 Author chain D； PDBConstruct 1–194； UniProt 27–220

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.

SAXS scattering curve SAXS Profile

P(r) Distance Distribution P(r) Distribution

Download Download SAXS (.dat) P(r) (.pr.out) CIF

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2. Structure Basics 2. Structure Basics

Entry ID entry_id	1gxd
Deposition date deposition_date	2002-04-02
Structure title title	proMMP-2/TIMP-2 complex
Keywords keywords	;HYDROLASE, METALLOPROTEASE, ZYMOGEN, COLLAGEN DEGRADATION, EXTRACELLULAR MATRIX, GELATINASE A, MATRIX METALLOPROTEINASE 2, PROTEINASE INHIBITOR ;; 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	58.32 Å
Radius of gyration Rg (electron density) rg_electron	60.97 Å
Forward intensity I(0) i0	499597000.00
Molecular weight molecular_weight	183980.0 kDa
Excluded volume excluded_volume	229270 Å³
Envelope volume envelope_volume	339210 Å³
Hydration-shell volume shell_volume	55882 Å³
Envelope diameter envelope_diameter	249.2 Å
Shell Rg shell_rg	47.37 Å
Envelope Rg envelope_rg	63.24 Å
Shape Rg shape_rg	60.87 Å
Total Rg total_rg	60.84 Å
Total atoms total_atoms	12945
Residues n_residues	1631
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	221.4 Å
Rg (real space) rg_real	59.78 Å
Rg uncertainty (real space) rg_real_error	3.00 Å
I(0) (real space) i0_real	4.9920e+08
I(0) uncertainty (real space) i0_real_error	1.1440e+07
Rg (reciprocal space) rg_reciprocal	56.94 Å
I(0) (reciprocal space) i0_reciprocal	497200000.0000
Solution quality estimate total_estimate	0.6636
Solution quality rating solution_quality	REASONABLE a REASONABLE solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	41.0 Å
Skewness Skewness skewness	0.858
Kurtosis Kurtosis kurtosis	0.225
Angular range angular_range	— – 0.1350 Å⁻¹
Current regularization parameter α current_alpha	0.0035
Highest regularization parameter α highest_alpha	26710000.0000
Real-space data points n_real_points	28
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.260; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.108; Smooth: 0.737

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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	72 KDA TYPE IV COLLAGENASE
Molecular weight formula_weight	70995.4 kDa
EC 编号 ec_number	3.4.24.24
Mutation mutation	YES
Source method src_method	man
Copy count entity_count	2

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B
Atom count atom_count	12945

APSPIIKFPGDVAPKTDKELAVQYLNTFYGCPKESCNLFVLKDTLKKMQKFFGLPQTGDLDQNTIETMRKPRCGNPDVANYNFFPRKPKWDKNQITYRIIGYTPDLDPETVDDAFARAFQVWSDVTPLRFSRIHDGEADIMINFGRWEHGDGYPFDGKDGLLAHAFAPGTGVGGDSHFDDDELWTLGEGQVVRVKYGNADGEYCKFPFLFNGKEYNSCTDTGRSDGFLWCSTTYNFEKDGKYGFCPHEALFTMGGNAEGQPCKFPFRFQGTSYDSCTTEGRTDGYRWCGTTEDYDRDKKYGFCPETAMSTVGGNSEGAPCVFPFTFLGNKYESCTSAGRSDGKMWCATTANYDDDRKWGFCPDQGYSLFLVAAHAFGHAMGLEHSQDPGALMAPIYTYTKNFRLSQDDIKGIQELYGASPDIDLGTGPTPTLGPVTPEICKQDIVFDGIAQIRGEIFFFKDRFIWRTVTPRDKPMGPLLVATFWPELPEKIDAVYEAPQEEKAVFFAGNEYWIYSASTLERGYPKPLTSLGLPPDVQRVDAAFNWSKNKKTYIFAGDKFWRYNEVKKKMDPGFPKLIADAWNAIPDNLDAVVDLQGGGHSYFFKGAYYLKLENQSLKSVKFGSIKSDWLGC

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	TRICHOPLUSIA NI

Entity 2 Entity 2 polymer

Description description	METALLOPROTEINASE INHIBITOR 2
Molecular weight formula_weight	21783.0 kDa
Source method src_method	man
Copy count entity_count	2

Polymer Polymer

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

CSCSPVHPQQAFCNADVVIRAKAVSEKEVDSGNDIYGNPIKRIQYEIKQIKMFKGPEKDIEFIYTAPSSAVCGVSLDVGGKKEYLIAGKAEGDGKMHITLCDFIVPWDTLSTTQKKSLNHRYQMGCECKITRCPMIPCYISSPDECLWMDWVTEKNINGHQAKFFACIKRSDGSCAWYRGAAPPKQEFLDIEDP

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	TRICHOPLUSIA NI

Entity 3 Entity 3 non-polymer

Description description	SULFATE ION
Molecular weight formula_weight	96.1 kDa
Source method src_method	syn
Copy count entity_count	2

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 non-polymer

Description description	CALCIUM ION
Molecular weight formula_weight	40.1 kDa
Source method src_method	syn
Copy count entity_count	2

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7. Fold Classification (SCOP + CATH) 28 domains

SCOP 2.08 (14 domains)

Domain ID domain_id	d1gxda1
Class class	a — All alpha proteins
Fold Fold fold	a.20 — PGBD-like
Superfamily Superfamily superfamily	a.20.1 — PGBD-like
Family Family family	a.20.1.2 — MMP N-terminal domain

Domain ID domain_id	d1gxda2
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.66.1.1 — Hemopexin-like domain

Domain ID domain_id	d1gxda3
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	d1gxda4
Class class	g — Small proteins
Fold Fold fold	g.14 — Kringle-like
Superfamily Superfamily superfamily	g.14.1 — Kringle-like
Family Family family	g.14.1.2 — Fibronectin type II module

Domain ID domain_id	d1gxda5
Class class	g — Small proteins
Fold Fold fold	g.14 — Kringle-like
Superfamily Superfamily superfamily	g.14.1 — Kringle-like
Family Family family	g.14.1.2 — Fibronectin type II module

Domain ID domain_id	d1gxda6
Class class	g — Small proteins
Fold Fold fold	g.14 — Kringle-like
Superfamily Superfamily superfamily	g.14.1 — Kringle-like
Family Family family	g.14.1.2 — Fibronectin type II module

Domain ID domain_id	d1gxdb1
Class class	a — All alpha proteins
Fold Fold fold	a.20 — PGBD-like
Superfamily Superfamily superfamily	a.20.1 — PGBD-like
Family Family family	a.20.1.2 — MMP N-terminal domain

Domain ID domain_id	d1gxdb2
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.66.1.1 — Hemopexin-like domain

Domain ID domain_id	d1gxdb3
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	d1gxdb4
Class class	g — Small proteins
Fold Fold fold	g.14 — Kringle-like
Superfamily Superfamily superfamily	g.14.1 — Kringle-like
Family Family family	g.14.1.2 — Fibronectin type II module

Domain ID domain_id	d1gxdb5
Class class	g — Small proteins
Fold Fold fold	g.14 — Kringle-like
Superfamily Superfamily superfamily	g.14.1 — Kringle-like
Family Family family	g.14.1.2 — Fibronectin type II module

Domain ID domain_id	d1gxdb6
Class class	g — Small proteins
Fold Fold fold	g.14 — Kringle-like
Superfamily Superfamily superfamily	g.14.1 — Kringle-like
Family Family family	g.14.1.2 — Fibronectin type II module

Domain ID domain_id	d1gxdc_
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	d1gxdd_
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

CATH v4.4 (14 domains)

Domain ID domain_id	1gxdA01
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	1gxdA02
Class class	2 — Mainly Beta
Architecture architecture	10 — Ribbon
Topology topology	10 — Seminal Fluid Protein PDC-109 (Domain B)
Homologous superfamily homologous superfamily	10 — Fibronectin, type II, collagen-binding

Domain ID domain_id	1gxdA03
Class class	2 — Mainly Beta
Architecture architecture	10 — Ribbon
Topology topology	10 — Seminal Fluid Protein PDC-109 (Domain B)
Homologous superfamily homologous superfamily	10 — Fibronectin, type II, collagen-binding

Domain ID domain_id	1gxdA04
Class class	2 — Mainly Beta
Architecture architecture	10 — Ribbon
Topology topology	10 — Seminal Fluid Protein PDC-109 (Domain B)
Homologous superfamily homologous superfamily	10 — Fibronectin, type II, collagen-binding

Domain ID domain_id	1gxdA05
Class class	2 — Mainly Beta
Architecture architecture	110 — 4 Propeller
Topology topology	10 — Hemopexin
Homologous superfamily homologous superfamily	10 — Hemopexin-like domain

Domain ID domain_id	1gxdB01
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	1gxdB02
Class class	2 — Mainly Beta
Architecture architecture	10 — Ribbon
Topology topology	10 — Seminal Fluid Protein PDC-109 (Domain B)
Homologous superfamily homologous superfamily	10 — Fibronectin, type II, collagen-binding

Domain ID domain_id	1gxdB03
Class class	2 — Mainly Beta
Architecture architecture	10 — Ribbon
Topology topology	10 — Seminal Fluid Protein PDC-109 (Domain B)
Homologous superfamily homologous superfamily	10 — Fibronectin, type II, collagen-binding

Domain ID domain_id	1gxdB04
Class class	2 — Mainly Beta
Architecture architecture	10 — Ribbon
Topology topology	10 — Seminal Fluid Protein PDC-109 (Domain B)
Homologous superfamily homologous superfamily	10 — Fibronectin, type II, collagen-binding

Domain ID domain_id	1gxdB05
Class class	2 — Mainly Beta
Architecture architecture	110 — 4 Propeller
Topology topology	10 — Hemopexin
Homologous superfamily homologous superfamily	10 — Hemopexin-like domain

Domain ID domain_id	1gxdC01
Class class	3 — Alpha Beta
Architecture architecture	90 — Alpha-Beta Complex
Topology topology	370 — Tissue inhibitor of metalloproteinase-1. Chain B, domain 1
Homologous superfamily homologous superfamily	10 — Tissue inhibitor of metalloproteinase-1. Chain B, domain 1

Domain ID domain_id	1gxdC02
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	1gxdD01
Class class	3 — Alpha Beta
Architecture architecture	90 — Alpha-Beta Complex
Topology topology	370 — Tissue inhibitor of metalloproteinase-1. Chain B, domain 1
Homologous superfamily homologous superfamily	10 — Tissue inhibitor of metalloproteinase-1. Chain B, domain 1

Domain ID domain_id	1gxdD02
Class class	2 — Mainly Beta
Architecture architecture	40 — Beta Barrel
Topology topology	50 — OB fold (Dihydrolipoamide Acetyltransferase, E2P)
Homologous superfamily homologous superfamily	120 —

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8. Citations (1)

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Unit-cell length a length_a	75.696 Å
Unit-cell length b length_b	374.575 Å
Unit-cell length c length_c	191.000 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	90.00 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	16

Space group space_group	C 2 2 21
Space-group number int_tables_number	20
Crystal system crystal_system	—

Resolution resolution	3.100 Å
Low-resolution limit resolution_low	8.000 Å
R factor r_factor	0.2780
R_work r_work	0.2750
R_free r_free	0.3330

fit	/app/data/saxs_computation/gx/1gxd/1gxd.fit
pddf	/app/data/pr_computation/gx/1gxd/1gxd.pr.out
profile	/app/data/saxs_computation/gx/1gxd/1gxd.dat

proMMP-2/TIMP-2 complex

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

72 KDA TYPE IV COLLAGENASE

State in the Current Structure

Other States of the Same Protein in the Database

METALLOPROTEINASE INHIBITOR 2

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 non-polymer

7. Fold Classification (SCOP + CATH) 28 domains

SCOP 2.08 (14 domains)

CATH v4.4 (14 domains)

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)