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- PDB-2c5d: Structure of a minimal Gas6-Axl complex -

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Basic information

Entry
Database: PDB / ID: 2c5d
TitleStructure of a minimal Gas6-Axl complex
Components
  • GROWTH-ARREST-SPECIFIC PROTEIN 6 PRECURSOR
  • TYROSINE-PROTEIN KINASE RECEPTOR UFO
KeywordsSIGNALING PROTEIN/RECEPTOR / GROWTH REGULATION-COMPLEX / VITAMIN K-DEPENDENT PROTEIN / LAMININ G-LIKE DOMAIN / RECEPTOR TYROSINE KINASE / IMMUNOGLOBULIN-LIKE DOMAIN / GROWTH REGULATION / EGF-LIKE DOMAIN / RECEPTOR / SIGNALING PROTEIN-RECEPTOR complex
Function / homology
Function and homology information


negative regulation of oligodendrocyte apoptotic process / negative regulation of renal albumin absorption / cellular response to vitamin K / forebrain cell migration / positive regulation of natural killer cell differentiation / hematopoietic stem cell migration to bone marrow / positive regulation of glomerular filtration / B cell chemotaxis / negative regulation of lymphocyte activation / cellular response to interferon-alpha ...negative regulation of oligodendrocyte apoptotic process / negative regulation of renal albumin absorption / cellular response to vitamin K / forebrain cell migration / positive regulation of natural killer cell differentiation / hematopoietic stem cell migration to bone marrow / positive regulation of glomerular filtration / B cell chemotaxis / negative regulation of lymphocyte activation / cellular response to interferon-alpha / positive regulation of pinocytosis / positive regulation of dendritic cell chemotaxis / extracellular matrix assembly / myeloid cell apoptotic process / negative regulation of macrophage cytokine production / neutrophil clearance / positive regulation of cytokine-mediated signaling pathway / natural killer cell differentiation / negative regulation of interleukin-1 production / secretion by cell / dendritic cell differentiation / positive regulation of viral life cycle / negative regulation of myeloid cell apoptotic process / negative regulation of biomineral tissue development / negative regulation of dendritic cell apoptotic process / negative regulation of fibroblast apoptotic process / cysteine-type endopeptidase inhibitor activity involved in apoptotic process / apoptotic cell clearance / fibroblast apoptotic process / ovulation cycle / erythrocyte homeostasis / phosphatidylserine binding / enzyme-linked receptor protein signaling pathway / myosin heavy chain binding / cell-substrate adhesion / vagina development / negative regulation of interleukin-6 production / negative regulation of type II interferon production / negative regulation of tumor necrosis factor production / blood vessel remodeling / negative regulation of tumor necrosis factor-mediated signaling pathway / positive regulation of TOR signaling / positive regulation of protein kinase activity / response to axon injury / phagocytosis / vascular endothelial growth factor receptor signaling pathway / animal organ regeneration / phosphatidylinositol 3-kinase binding / Transport of gamma-carboxylated protein precursors from the endoplasmic reticulum to the Golgi apparatus / Gamma-carboxylation of protein precursors / negative regulation of endothelial cell apoptotic process / Removal of aminoterminal propeptides from gamma-carboxylated proteins / cell maturation / activation of protein kinase B activity / positive regulation of phagocytosis / transmembrane receptor protein tyrosine kinase activity / substrate adhesion-dependent cell spreading / viral genome replication / cell surface receptor protein tyrosine kinase signaling pathway / platelet alpha granule lumen / cellular response to starvation / positive regulation of protein export from nucleus / protein localization to plasma membrane / Cell surface interactions at the vascular wall / establishment of localization in cell / Post-translational protein phosphorylation / placental growth factor receptor activity / cellular response to glucose stimulus / insulin receptor activity / vascular endothelial growth factor receptor activity / hepatocyte growth factor receptor activity / macrophage colony-stimulating factor receptor activity / platelet-derived growth factor alpha-receptor activity / platelet-derived growth factor beta-receptor activity / stem cell factor receptor activity / boss receptor activity / protein tyrosine kinase collagen receptor activity / brain-derived neurotrophic factor receptor activity / transmembrane-ephrin receptor activity / GPI-linked ephrin receptor activity / epidermal growth factor receptor activity / fibroblast growth factor receptor activity / insulin-like growth factor receptor activity / receptor protein-tyrosine kinase / cellular response to growth factor stimulus / calcium ion transmembrane transport / receptor tyrosine kinase binding / platelet activation / Golgi lumen / cellular response to hydrogen peroxide / VEGFA-VEGFR2 Pathway / positive regulation of fibroblast proliferation / Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs) / neuron migration / blood coagulation / Platelet degranulation / cellular response to xenobiotic stimulus / cell migration / nervous system development / actin cytoskeleton
Similarity search - Function
: / Laminin G domain / Complement Clr-like EGF domain / Complement Clr-like EGF-like / Laminin G domain / EGF-like, conserved site / Human growth factor-like EGF / Laminin G domain profile. / Laminin G domain / Laminin G domain ...: / Laminin G domain / Complement Clr-like EGF domain / Complement Clr-like EGF-like / Laminin G domain / EGF-like, conserved site / Human growth factor-like EGF / Laminin G domain profile. / Laminin G domain / Laminin G domain / : / Calcium-binding EGF domain / Coagulation factor-like, Gla domain superfamily / Immunoglobulin domain / EGF-type aspartate/asparagine hydroxylation site / EGF-like calcium-binding, conserved site / Calcium-binding EGF-like domain signature. / Aspartic acid and asparagine hydroxylation site. / EGF-like calcium-binding domain / Calcium-binding EGF-like domain / Vitamin K-dependent carboxylation/gamma-carboxyglutamic (GLA) domain / Gamma-carboxyglutamic acid-rich (GLA) domain / Gamma-carboxyglutamic acid-rich (GLA) domain superfamily / Vitamin K-dependent carboxylation domain. / Gla domain profile. / Domain containing Gla (gamma-carboxyglutamate) residues. / Epidermal growth factor-like domain. / Jelly Rolls - #200 / EGF-like domain profile. / Growth factor receptor cysteine-rich domain superfamily / Fibronectin type III domain / EGF-like domain signature 1. / : / EGF-like domain signature 2. / EGF-like domain / Fibronectin type 3 domain / Fibronectin type-III domain profile. / Fibronectin type III / Fibronectin type III superfamily / Tyrosine-protein kinase, catalytic domain / Tyrosine kinase, catalytic domain / Tyrosine protein kinases specific active-site signature. / Tyrosine-protein kinase, active site / Immunoglobulin subtype / Immunoglobulin / Concanavalin A-like lectin/glucanase domain superfamily / Serine-threonine/tyrosine-protein kinase, catalytic domain / Protein tyrosine and serine/threonine kinase / Ig-like domain profile. / Immunoglobulin-like domain / Immunoglobulin-like domain superfamily / Jelly Rolls / Protein kinase, ATP binding site / Protein kinases ATP-binding region signature. / Immunoglobulin-like fold / Protein kinase domain profile. / Protein kinase domain / Immunoglobulins / Protein kinase-like domain superfamily / Immunoglobulin-like / Sandwich / Mainly Beta
Similarity search - Domain/homology
NICKEL (II) ION / Tyrosine-protein kinase receptor UFO / Growth arrest-specific protein 6
Similarity search - Component
Biological speciesHOMO SAPIENS (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 3.3 Å
AuthorsSasaki, T. / Knyazev, P.G. / Clout, N.J. / Cheburkin, Y. / Goehring, W. / Ullrich, A. / Timpl, R. / Hohenester, E.
Citation
#1: Journal: J.Biol.Chem. / Year: 2002
Title: Crystal Structure of a C-Terminal Fragment of Growth Arrest-Specific Protein Gas6
Authors: Sasaki, T. / Knyazev, P.G. / Cheburkin, Y. / Goehring, W. / Tisi, D. / Ullrich, A. / Timpl, R. / Hohenester, E.
#2: Journal: J.Biol.Chem. / Year: 2004
Title: Ligand Recognition and Homophilic Interactions in Tyro3
Authors: Heiring, C. / Dahlback, B. / Muller, Y.A.
History
DepositionOct 26, 2005Deposition site: PDBE / Processing site: PDBE
Revision 1.0Dec 19, 2005Provider: repository / Type: Initial release
Revision 1.1May 8, 2011Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 2.0Jul 29, 2020Group: Atomic model / Data collection ...Atomic model / Data collection / Derived calculations / Other / Structure summary
Category: atom_site / chem_comp ...atom_site / chem_comp / entity / pdbx_branch_scheme / pdbx_chem_comp_identifier / pdbx_database_status / pdbx_entity_branch / pdbx_entity_branch_descriptor / pdbx_entity_branch_link / pdbx_entity_branch_list / pdbx_entity_nonpoly / pdbx_nonpoly_scheme / pdbx_struct_assembly_gen / pdbx_struct_conn_angle / struct_asym / struct_conn / struct_site / struct_site_gen
Item: _atom_site.B_iso_or_equiv / _atom_site.Cartn_x ..._atom_site.B_iso_or_equiv / _atom_site.Cartn_x / _atom_site.Cartn_y / _atom_site.Cartn_z / _atom_site.auth_asym_id / _atom_site.auth_atom_id / _atom_site.auth_comp_id / _atom_site.auth_seq_id / _atom_site.label_asym_id / _atom_site.label_atom_id / _atom_site.label_comp_id / _atom_site.label_entity_id / _atom_site.type_symbol / _chem_comp.name / _chem_comp.type / _entity.formula_weight / _entity.pdbx_description / _entity.pdbx_number_of_molecules / _entity.src_method / _entity.type / _pdbx_database_status.status_code_sf / _pdbx_struct_assembly_gen.asym_id_list / _pdbx_struct_conn_angle.ptnr1_auth_asym_id / _pdbx_struct_conn_angle.ptnr1_auth_comp_id / _pdbx_struct_conn_angle.ptnr1_auth_seq_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.ptnr1_symmetry / _pdbx_struct_conn_angle.ptnr2_label_asym_id / _pdbx_struct_conn_angle.ptnr3_auth_asym_id / _pdbx_struct_conn_angle.ptnr3_auth_comp_id / _pdbx_struct_conn_angle.ptnr3_auth_seq_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.ptnr3_symmetry / _pdbx_struct_conn_angle.value / _struct_conn.conn_type_id / _struct_conn.id / _struct_conn.pdbx_dist_value / _struct_conn.pdbx_leaving_atom_flag / _struct_conn.pdbx_role / _struct_conn.ptnr1_auth_asym_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.ptnr1_symmetry / _struct_conn.ptnr2_auth_asym_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_conn.ptnr2_label_seq_id / _struct_conn.ptnr2_symmetry
Description: Carbohydrate remediation / Provider: repository / Type: Remediation
Revision 2.1Dec 13, 2023Group: Data collection / Database references ...Data collection / Database references / Refinement description / Structure summary
Category: chem_comp / chem_comp_atom ...chem_comp / chem_comp_atom / chem_comp_bond / database_2 / pdbx_initial_refinement_model
Item: _chem_comp.pdbx_synonyms / _database_2.pdbx_DOI / _database_2.pdbx_database_accession
Revision 2.2Nov 20, 2024Group: Structure summary / Category: pdbx_entry_details / pdbx_modification_feature
Remark 700 SHEET THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN ORDER TO REPRESENT THIS FEATURE IN ... SHEET THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN ORDER TO REPRESENT THIS FEATURE IN THE SHEET RECORDS BELOW, TWO SHEETS ARE DEFINED.

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: GROWTH-ARREST-SPECIFIC PROTEIN 6 PRECURSOR
B: GROWTH-ARREST-SPECIFIC PROTEIN 6 PRECURSOR
C: TYROSINE-PROTEIN KINASE RECEPTOR UFO
D: TYROSINE-PROTEIN KINASE RECEPTOR UFO
hetero molecules


Theoretical massNumber of molelcules
Total (without water)136,62011
Polymers135,4784
Non-polymers1,1427
Water00
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPQS
Unit cell
Length a, b, c (Å)292.951, 292.951, 63.951
Angle α, β, γ (deg.)90.00, 90.00, 120.00
Int Tables number169
Space group name H-MP61
Noncrystallographic symmetry (NCS)NCS oper:
IDCodeMatrixVector
1given(0.07122, 0.99736, 0.01392), (0.99745, -0.07115, -0.0052), (-0.00419, 0.01426, -0.99989)-1.68797, 1.21185, 183.00417
2given(0.07122, 0.99736, 0.01392), (0.99745, -0.07115, -0.0052), (-0.00419, 0.01426, -0.99989)-1.68797, 1.21185, 183.00417

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Components

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Protein , 2 types, 4 molecules ABCD

#1: Protein GROWTH-ARREST-SPECIFIC PROTEIN 6 PRECURSOR / GAS-6


Mass: 46615.352 Da / Num. of mol.: 2 / Fragment: LG DOMAINS, RESIDUES 207-624
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) HOMO SAPIENS (human) / Cell line (production host): 293-EBNA / Production host: HOMO SAPIENS (human) / References: UniProt: Q14393
#2: Protein TYROSINE-PROTEIN KINASE RECEPTOR UFO / AXL ONCOGENE


Mass: 21123.408 Da / Num. of mol.: 2 / Fragment: IG DOMAINS, RESIDUES 26-220
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) HOMO SAPIENS (human) / Plasmid: PASK-IBA12 / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): BL21 / References: UniProt: P30530, EC: 2.7.1.112

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Sugars , 1 types, 2 molecules

#3: Polysaccharide 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose


Type: oligosaccharide / Mass: 424.401 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
DescriptorTypeProgram
DGlcpNAcb1-4DGlcpNAcb1-Glycam Condensed SequenceGMML 1.0
WURCS=2.0/1,2,1/[a2122h-1b_1-5_2*NCC/3=O]/1-1/a4-b1WURCSPDB2Glycan 1.1.0
[]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-GlcpNAc]{}}}LINUCSPDB-CARE

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Non-polymers , 3 types, 5 molecules

#4: Chemical ChemComp-CA / CALCIUM ION


Mass: 40.078 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: Ca
#5: Chemical ChemComp-NI / NICKEL (II) ION


Mass: 58.693 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: Ni
#6: Chemical ChemComp-SO4 / SULFATE ION


Mass: 96.063 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: SO4

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Details

Has protein modificationY

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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: 5.3 Å3/Da / Density % sol: 78 %
Crystal growpH: 7.5 / Details: pH 7.50

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: ESRF / Beamline: ID23-1 / Wavelength: 0.9794
DetectorType: MARRESEARCH / Detector: CCD / Date: Mar 11, 2005
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.9794 Å / Relative weight: 1
ReflectionResolution: 3.3→20 Å / Num. obs: 47655 / % possible obs: 99.5 % / Observed criterion σ(I): 0 / Redundancy: 5.9 % / Rmerge(I) obs: 0.12 / Net I/σ(I): 11.3
Reflection shellResolution: 3.3→3.48 Å / Redundancy: 5.8 % / Rmerge(I) obs: 0.43 / Mean I/σ(I) obs: 3.7 / % possible all: 100

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Processing

Software
NameVersionClassification
CNS1.1refinement
MOSFLMdata reduction
SCALAdata scaling
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: PDB ENTRIES 1H30 AND 1RHF

1h30

1rhf


Resolution: 3.3→20 Å / Data cutoff high absF: 10000 / Isotropic thermal model: RESTRAINED / Cross valid method: THROUGHOUT / σ(F): 0 / Stereochemistry target values: MAXIMUM LIKELIHOOD
RfactorNum. reflection% reflectionSelection details
Rfree0.2653 2384 5 %RANDOM
Rwork0.2409 ---
obs0.2409 47648 99.9 %-
Solvent computationSolvent model: FLAT / Bsol: 10 Å2 / ksol: 0.209994 e/Å3
Displacement parameters
Baniso -1Baniso -2Baniso -3
1--7.163 Å2-6.701 Å20 Å2
2---7.163 Å20 Å2
3---14.325 Å2
Refinement stepCycle: LAST / Resolution: 3.3→20 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms8814 0 65 0 8879
Refine LS restraints
Refine-IDTypeDev idealDev ideal target
X-RAY DIFFRACTIONc_bond_d0.009
X-RAY DIFFRACTIONc_bond_d_na
X-RAY DIFFRACTIONc_bond_d_prot
X-RAY DIFFRACTIONc_angle_d
X-RAY DIFFRACTIONc_angle_d_na
X-RAY DIFFRACTIONc_angle_d_prot
X-RAY DIFFRACTIONc_angle_deg1.5
X-RAY DIFFRACTIONc_angle_deg_na
X-RAY DIFFRACTIONc_angle_deg_prot
X-RAY DIFFRACTIONc_dihedral_angle_d
X-RAY DIFFRACTIONc_dihedral_angle_d_na
X-RAY DIFFRACTIONc_dihedral_angle_d_prot
X-RAY DIFFRACTIONc_improper_angle_d
X-RAY DIFFRACTIONc_improper_angle_d_na
X-RAY DIFFRACTIONc_improper_angle_d_prot
X-RAY DIFFRACTIONc_mcbond_it1.721.5
X-RAY DIFFRACTIONc_mcangle_it2.012
X-RAY DIFFRACTIONc_scbond_it3.142
X-RAY DIFFRACTIONc_scangle_it3.52.5
Xplor file
Refine-IDSerial noParam fileTopol file
X-RAY DIFFRACTION1PROTEIN_REP.PARAMPROTEIN.TOP
X-RAY DIFFRACTION2ION.PARAMION.TOP
X-RAY DIFFRACTION3CARBOHYDRATE.PARAMCARBOHYDRATE.TOP

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