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- PDB-3ljg: Human MMP12 in complex with non-zinc chelating inhibitor -

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Basic information

Entry
Database: PDB / ID: 3ljg
TitleHuman MMP12 in complex with non-zinc chelating inhibitor
ComponentsMacrophage metalloelastase
KeywordsHYDROLASE/HYDROLASE INHIBITOR / MMP12 elastase non-chelating inhibitor / HYDROLASE / HYDROLASE-HYDROLASE INHIBITOR complex
Function / homology
Function and homology information


macrophage elastase / negative regulation of endothelial cell-matrix adhesion via fibronectin / bronchiole development / positive regulation of epithelial cell proliferation involved in wound healing / elastin catabolic process / regulation of defense response to virus by host / positive regulation of type I interferon-mediated signaling pathway / wound healing, spreading of epidermal cells / negative regulation of type I interferon-mediated signaling pathway / lung alveolus development ...macrophage elastase / negative regulation of endothelial cell-matrix adhesion via fibronectin / bronchiole development / positive regulation of epithelial cell proliferation involved in wound healing / elastin catabolic process / regulation of defense response to virus by host / positive regulation of type I interferon-mediated signaling pathway / wound healing, spreading of epidermal cells / negative regulation of type I interferon-mediated signaling pathway / lung alveolus development / response to amyloid-beta / Collagen degradation / collagen catabolic process / extracellular matrix disassembly / positive regulation of interferon-alpha production / core promoter sequence-specific DNA binding / collagen binding / Degradation of the extracellular matrix / extracellular matrix organization / extracellular matrix / cellular response to virus / metalloendopeptidase activity / protein import into nucleus / endopeptidase activity / sequence-specific DNA binding / serine-type endopeptidase activity / calcium ion binding / negative regulation of transcription by RNA polymerase II / positive regulation of transcription by RNA polymerase II / proteolysis / extracellular space / zinc ion binding / extracellular region / nucleus / cytoplasm
Similarity search - Function
Peptidoglycan binding-like / Hemopexin, conserved site / Hemopexin domain signature. / Hemopexin-like domain / Peptidase M10A, cysteine switch, zinc binding site / Matrixins cysteine switch. / Putative peptidoglycan binding domain / Hemopexin-like repeats / Hemopexin-like domain superfamily / Hemopexin ...Peptidoglycan binding-like / Hemopexin, conserved site / Hemopexin domain signature. / Hemopexin-like domain / Peptidase M10A, cysteine switch, zinc binding site / Matrixins cysteine switch. / Putative peptidoglycan binding domain / Hemopexin-like repeats / Hemopexin-like domain superfamily / Hemopexin / Hemopexin repeat profile. / Hemopexin-like repeats. / Peptidase M10A / Peptidase M10A, catalytic domain / Peptidase M10, metallopeptidase / Matrixin / PGBD-like superfamily / Peptidase, metallopeptidase / Zinc-dependent metalloprotease / Collagenase (Catalytic Domain) / Collagenase (Catalytic Domain) / Metallopeptidase, catalytic domain superfamily / Neutral zinc metallopeptidases, zinc-binding region signature. / 3-Layer(aba) Sandwich / Alpha Beta
Similarity search - Domain/homology
N-(3-BIPHENYL-4-YLPROPANOYL)-L-ALPHA-GLUTAMYL-L-ALPHA-GLUTAMYL-AMIDE / Chem-EEF / ACETOHYDROXAMIC ACID / Macrophage metalloelastase
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / rigid body / Resolution: 1.313 Å
AuthorsStura, E.A. / Dive, V. / Devel, L. / Vera, L. / Beau, F.
CitationJournal: J.Biol.Chem. / Year: 2010
Title: Insights from selective non-phosphinic inhibitors of MMP-12 tailored to fit with an S1' loop canonical conformation.
Authors: Devel, L. / Garcia, S. / Czarny, B. / Beau, F. / LaJeunesse, E. / Vera, L. / Georgiadis, D. / Stura, E. / Dive, V.
History
DepositionJan 26, 2010Deposition site: RCSB / Processing site: RCSB
Revision 1.0Sep 1, 2010Provider: repository / Type: Initial release
Revision 1.1Jul 13, 2011Group: Version format compliance
Revision 1.2Dec 12, 2012Group: Other
Revision 2.0Jul 17, 2019Group: Atomic model / Data collection / Refinement description
Category: atom_site / software
Item: _atom_site.occupancy / _software.classification ..._atom_site.occupancy / _software.classification / _software.name / _software.version
Revision 2.1Sep 6, 2023Group: Data collection / Database references ...Data collection / Database references / Derived calculations / Refinement description
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_initial_refinement_model / pdbx_struct_conn_angle / struct_conn / struct_ref_seq_dif / struct_site
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_struct_conn_angle.ptnr1_auth_comp_id / _pdbx_struct_conn_angle.ptnr1_auth_seq_id / _pdbx_struct_conn_angle.ptnr1_label_alt_id / _pdbx_struct_conn_angle.ptnr1_label_asym_id / _pdbx_struct_conn_angle.ptnr1_label_atom_id / _pdbx_struct_conn_angle.ptnr1_label_comp_id / _pdbx_struct_conn_angle.ptnr1_label_seq_id / _pdbx_struct_conn_angle.ptnr2_auth_comp_id / _pdbx_struct_conn_angle.ptnr2_auth_seq_id / _pdbx_struct_conn_angle.ptnr2_label_asym_id / _pdbx_struct_conn_angle.ptnr2_label_atom_id / _pdbx_struct_conn_angle.ptnr2_label_comp_id / _pdbx_struct_conn_angle.ptnr3_auth_comp_id / _pdbx_struct_conn_angle.ptnr3_auth_seq_id / _pdbx_struct_conn_angle.ptnr3_label_alt_id / _pdbx_struct_conn_angle.ptnr3_label_asym_id / _pdbx_struct_conn_angle.ptnr3_label_atom_id / _pdbx_struct_conn_angle.ptnr3_label_comp_id / _pdbx_struct_conn_angle.ptnr3_label_seq_id / _pdbx_struct_conn_angle.value / _struct_conn.pdbx_dist_value / _struct_conn.pdbx_ptnr2_label_alt_id / _struct_conn.ptnr1_auth_comp_id / _struct_conn.ptnr1_auth_seq_id / _struct_conn.ptnr1_label_asym_id / _struct_conn.ptnr1_label_atom_id / _struct_conn.ptnr1_label_comp_id / _struct_conn.ptnr1_label_seq_id / _struct_conn.ptnr2_auth_comp_id / _struct_conn.ptnr2_auth_seq_id / _struct_conn.ptnr2_label_asym_id / _struct_conn.ptnr2_label_atom_id / _struct_conn.ptnr2_label_comp_id / _struct_ref_seq_dif.details / _struct_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Macrophage metalloelastase
hetero molecules


Theoretical massNumber of molelcules
Total (without water)18,99010
Polymers17,6161
Non-polymers1,3749
Water5,891327
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPISA
Unit cell
Length a, b, c (Å)69.090, 62.820, 37.550
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number18
Space group name H-MP21212
Components on special symmetry positions
IDModelComponents
11A-304-

P6G

21A-52-

HOH

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Components

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Protein , 1 types, 1 molecules A

#1: Protein Macrophage metalloelastase / MME / Matrix metalloproteinase-12 / MMP-12 / Macrophage elastase / ME / hME


Mass: 17615.670 Da / Num. of mol.: 1 / Fragment: MMP-12 catalitic subunit (RESIDUES 106-263) / Mutation: F171D
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: MMP12, HME / Production host: Escherichia coli (E. coli) / Strain (production host): BL21 / References: UniProt: P39900, macrophage elastase

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Non-polymers , 6 types, 336 molecules

#2: Chemical ChemComp-ZN / ZINC ION


Mass: 65.409 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: Zn
#3: Chemical ChemComp-CA / CALCIUM ION


Mass: 40.078 Da / Num. of mol.: 3 / Source method: obtained synthetically / Formula: Ca
#4: Chemical ChemComp-HAE / ACETOHYDROXAMIC ACID


Mass: 75.067 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C2H5NO2 / Comment: inhibitor, medication*YM
#5: Chemical ChemComp-EEF / N-(3-biphenyl-4-ylpropanoyl)-L-alpha-glutamyl-L-alpha-glutamyl-amide


Type: peptide-like, Peptide-like / Class: Inhibitor / Mass: 483.514 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C25H29N3O7
References: N-(3-BIPHENYL-4-YLPROPANOYL)-L-ALPHA-GLUTAMYL-L-ALPHA-GLUTAMYL-AMIDE
#6: Chemical ChemComp-P6G / HEXAETHYLENE GLYCOL / POLYETHYLENE GLYCOL PEG400


Mass: 282.331 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C12H26O7 / Comment: precipitant*YM
#7: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 327 / Source method: isolated from a natural source / Formula: H2O

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Experimental details

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Experiment

ExperimentMethod: X-RAY DIFFRACTION / Number of used crystals: 1

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Sample preparation

CrystalDensity Matthews: 2.31 Å3/Da / Density % sol: 46.82 %
Crystal growTemperature: 298 K / Method: vapor diffusion, sitting drop / pH: 8.5
Details: MMP12 at 4mg/ml co-crystallization with AHA and non-chelating inhibitor with precipitant: 19% PEG 10K, 0.2M imidazole malate, pH 8.5, VAPOR DIFFUSION, SITTING DROP, temperature 298K

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: SOLEIL / Beamline: PROXIMA 1 / Wavelength: 0.855 Å
DetectorType: ADSC QUANTUM 315r / Detector: CCD / Date: Feb 5, 2009 / Details: mirrors
RadiationMonochromator: Si 111 CHANNEL / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.855 Å / Relative weight: 1
ReflectionResolution: 1.31→32.99 Å / Num. all: 39828 / Num. obs: 39828 / % possible obs: 100 % / Observed criterion σ(F): 1 / Observed criterion σ(I): 2 / Redundancy: 9.2 % / Rmerge(I) obs: 0.101 / Rsym value: 0.107 / Net I/σ(I): 13.6
Reflection shellResolution: 1.31→1.38 Å / Redundancy: 9.3 % / Rmerge(I) obs: 0.766 / Mean I/σ(I) obs: 2.9 / Rsym value: 0.811 / % possible all: 100

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Processing

Software
NameVersionClassification
PHENIX(phenix.refine)refinement
REFMAC(rigid body)refinement
DNAdata collection
MOSFLMdata reduction
SCALAdata scaling
REFMAC(rigid body)phasing
RefinementMethod to determine structure: rigid body
Starting model: PDB ENTRY 3LIR

3lir


Resolution: 1.313→28.594 Å / SU ML: 0.13 / Isotropic thermal model: Isotropic / σ(F): 1.44 / Phase error: 18.99 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.1948 1998 5.02 %
Rwork0.1726 --
obs0.1738 39775 99.96 %
all-39775 -
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL / Bsol: 48.009 Å2 / ksol: 0.327 e/Å3
Displacement parameters
Baniso -1Baniso -2Baniso -3
1--0.1565 Å20 Å20 Å2
2---0.0519 Å2-0 Å2
3---0.2084 Å2
Refinement stepCycle: LAST / Resolution: 1.313→28.594 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms1246 0 59 327 1632
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.0071406
X-RAY DIFFRACTIONf_angle_d1.091903
X-RAY DIFFRACTIONf_dihedral_angle_d18.144518
X-RAY DIFFRACTIONf_chiral_restr0.072192
X-RAY DIFFRACTIONf_plane_restr0.019247
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
1.313-1.34580.28061480.29792643X-RAY DIFFRACTION100
1.3458-1.38220.29721400.2622669X-RAY DIFFRACTION100
1.3822-1.42290.24421310.23692647X-RAY DIFFRACTION100
1.4229-1.46880.22161300.22542672X-RAY DIFFRACTION100
1.4688-1.52130.21781440.19362670X-RAY DIFFRACTION100
1.5213-1.58220.22831170.18772689X-RAY DIFFRACTION100
1.5822-1.65420.21061460.18122676X-RAY DIFFRACTION100
1.6542-1.74140.23521390.16812692X-RAY DIFFRACTION100
1.7414-1.85050.19341400.16492683X-RAY DIFFRACTION100
1.8505-1.99340.19571640.1552676X-RAY DIFFRACTION100
1.9934-2.19390.17781440.1472700X-RAY DIFFRACTION100
2.1939-2.51120.18021320.15772757X-RAY DIFFRACTION100
2.5112-3.16320.17371420.15562754X-RAY DIFFRACTION100
3.1632-28.60050.16351810.1512849X-RAY DIFFRACTION100

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