2uzy

Structure of the human receptor tyrosine kinase Met in complex with the Listeria monocytogenes invasion protein inlb: low resolution, Crystal form II

Method: X-RAY DIFFRACTION Dmax: 146.1 Å Quality: GOOD

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

INTERNALIN B

LISTERIA MONOCYTOGENES

UniProt P25147

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 36–321 Fragment:INTERNALIN DOMAIN (CAP, LRR, IR)\: INLB321, RESIDUES 36-321 HEPATOCYTE GROWTH FACTOR RECEPTOR × 1 (P08581) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;298 K;VAPOR DIFFUSION AT 25 DEGREE C IN SITTING-DROPS. 2 UL PROTEIN (8 MG/ML)PLUS 2 UL RESERVOIR (1.4 M NA/K PHOSPHATE, PH 6.5, 10% PEG 2000 MONO-METHYL-ETHER) Resolution 4.00 Å R-free 0.301
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain C; UniProt 36–321 Fragment:INTERNALIN DOMAIN (CAP, LRR, IR)\: INLB321, RESIDUES 36-321 HEPATOCYTE GROWTH FACTOR RECEPTOR × 1 (P08581) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;298 K;VAPOR DIFFUSION AT 25 DEGREE C IN SITTING-DROPS. 2 UL PROTEIN (8 MG/ML)PLUS 2 UL RESERVOIR (1.4 M NA/K PHOSPHATE, PH 6.5, 10% PEG 2000 MONO-METHYL-ETHER) Resolution 4.00 Å R-free 0.301

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.

16 other PDB entries and 33 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name INLB_LISMO
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 4–289; UniProt 36–321 Author chain C; PDBConstruct 4–289; UniProt 36–321

HEPATOCYTE GROWTH FACTOR RECEPTOR

HOMO SAPIENS

UniProt P08581

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 B; UniProt 25–740 Fragment:SEMA, PSI, IG1, IG2\: MET741, RESIDUES 25-740 INTERNALIN B × 1 (P25147) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;298 K;VAPOR DIFFUSION AT 25 DEGREE C IN SITTING-DROPS. 2 UL PROTEIN (8 MG/ML)PLUS 2 UL RESERVOIR (1.4 M NA/K PHOSPHATE, PH 6.5, 10% PEG 2000 MONO-METHYL-ETHER) Resolution 4.00 Å R-free 0.301
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain D; UniProt 25–740 Fragment:SEMA, PSI, IG1, IG2\: MET741, RESIDUES 25-740 INTERNALIN B × 1 (P25147) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;298 K;VAPOR DIFFUSION AT 25 DEGREE C IN SITTING-DROPS. 2 UL PROTEIN (8 MG/ML)PLUS 2 UL RESERVOIR (1.4 M NA/K PHOSPHATE, PH 6.5, 10% PEG 2000 MONO-METHYL-ETHER) Resolution 4.00 Å R-free 0.301

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.

128 other PDB entries and 165 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name MET_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 4–719; UniProt 25–740 Author chain D; PDBConstruct 4–719; UniProt 25–740

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

SAXS profile for 2uzy

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 2uzy
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2. Structure Basics 2. Structure Basics

Entry ID entry_id2uzy
Deposition date deposition_date2007-05-02
Structure title titleStructure of the human receptor tyrosine kinase Met in complex with the Listeria monocytogenes invasion protein inlb: low resolution, Crystal form II
Keywords keywords;SIGNALING PROTEIN/RECEPTOR, LEUCINE RICH REPEAT, RECEPTOR ECTODOMAIN, HEPATOCYTE GROWTH FACTOR RECEPTOR, ATP-BINDING, TRANSFERASE, POLYMORPHISM, GLYCOPROTEIN, VIRULENCE FACTOR, DISEASE MUTATION, NUCLEOTIDE-BINDING, TRANSMEMBRANE, PROTO-ONCOGENE, PHOSPHORYLATION, LEUCINE-RICH REPEAT, ALTERNATIVE SPLICING, TYROSINE-PROTEIN KINASE, CHROMOSOMAL REARRANGEMENT, LRR, HGFR, KINASE, MEMBRANE, RECEPTOR, INTERNALIN, SIGNALING PROTEIN-RECEPTOR COMPLEX ;; SIGNALING PROTEIN/RECEPTOR
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier43.61
Radius of gyration Rg (electron density) rg_electron43.33
Forward intensity I(0) i0597055000.00
Molecular weight molecular_weight203660.0 kDa
Excluded volume excluded_volume256110 ų
Envelope volume envelope_volume363140 ų
Hydration-shell volume shell_volume69254 ų
Envelope diameter envelope_diameter162.2
Shell Rg shell_rg49.03
Envelope Rg envelope_rg42.31
Shape Rg shape_rg43.30
Total Rg total_rg43.71
Total atoms total_atoms14329
Residues n_residues1820
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 −1
Data points n_points101
Shell type shell_typedirectional
Solvent electron density solvent_density0.3340 e/ų
Shell contrast contrast_shell0.0300 e/ų
CRYSOL version crysol_version4.1.3

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

Maximum dimension Dmax dmax146.1
Rg (real space) rg_real43.52
Rg uncertainty (real space) rg_real_error1.33
I(0) (real space) i0_real5.9710e+08
I(0) uncertainty (real space) i0_real_error1.1540e+07
Rg (reciprocal space) rg_reciprocal43.61
I(0) (reciprocal space) i0_reciprocal597100000.0000
Solution quality estimate total_estimate0.8771
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary56.8
Skewness Skewness skewness0.270
Kurtosis Kurtosis kurtosis-0.247
Angular range angular_range— – 0.1800 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha67770000.0000
Real-space data points n_real_points37
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.854; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.837

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

7. Fold Classification (SCOP + CATH) 12 domains

CATH v4.4 (12 domains)

Domain ID domain_id2uzyA01
Class class3 — Alpha Beta
Architecture architecture80 — Alpha-Beta Horseshoe
Topology topology10 — Leucine-rich repeat, LRR (right-handed beta-alpha superhelix)
Homologous superfamily homologous superfamily10 — Ribonuclease Inhibitor
Domain ID domain_id2uzyA02
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily1220
Domain ID domain_id2uzyB01
Class class2 — Mainly Beta
Architecture architecture130 — 7 Propeller
Topology topology10 — Methylamine Dehydrogenase; Chain H
Homologous superfamily homologous superfamily10 — YVTN repeat-like/Quinoprotein amine dehydrogenase
Domain ID domain_id2uzyB02
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology1680 — ligand-binding face of the semaphorins, domain 2
Homologous superfamily homologous superfamily10 — ligand-binding face of the semaphorins, domain 2
Domain ID domain_id2uzyB03
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id2uzyB04
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id2uzyC01
Class class3 — Alpha Beta
Architecture architecture80 — Alpha-Beta Horseshoe
Topology topology10 — Leucine-rich repeat, LRR (right-handed beta-alpha superhelix)
Homologous superfamily homologous superfamily10 — Ribonuclease Inhibitor
Domain ID domain_id2uzyC02
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily1220
Domain ID domain_id2uzyD01
Class class2 — Mainly Beta
Architecture architecture130 — 7 Propeller
Topology topology10 — Methylamine Dehydrogenase; Chain H
Homologous superfamily homologous superfamily10 — YVTN repeat-like/Quinoprotein amine dehydrogenase
Domain ID domain_id2uzyD02
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology1680 — ligand-binding face of the semaphorins, domain 2
Homologous superfamily homologous superfamily10 — ligand-binding face of the semaphorins, domain 2
Domain ID domain_id2uzyD03
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id2uzyD04
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins

8. Citations (1)

9. Files and Curves (10)