5abz

Complex of the FimH lectin with a C-linked naphtyl alpha-D-mannoside in soaked trigonal crystals at 2.40 A resolution

Method: X-RAY DIFFRACTION Dmax: 67.7 Å Quality: EXCELLENT

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

FIMH

ESCHERICHIA COLI

UniProt P08191

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 22–179 Fragment:LECTIN DOMAIN, UNP RESIDUES 22-179 Z47 (2R,3S,4R,5S,6R)-2-(HYDROXYMETHYL)-6-[3-(NAPHTHALEN-1-YL)PROPYL]OXANE-3,4,5-TRIOL × 1 NI NICKEL (II) ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:pH 8.6;PH 8.6 Resolution 2.40 Å R-free 0.206
2 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain B; UniProt 22–179 Fragment:LECTIN DOMAIN, UNP RESIDUES 22-179 Z47 (2R,3S,4R,5S,6R)-2-(HYDROXYMETHYL)-6-[3-(NAPHTHALEN-1-YL)PROPYL]OXANE-3,4,5-TRIOL × 1 NI NICKEL (II) ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:pH 8.6;PH 8.6 Resolution 2.40 Å R-free 0.206

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.

57 other PDB entries and 137 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name FIMH_ECOLI
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–158; UniProt 22–179 Author chain B; PDBConstruct 1–158; UniProt 22–179

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 5abz

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 5abz
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2. Structure Basics 2. Structure Basics

Entry ID entry_id5abz
Deposition date deposition_date2015-08-10
Structure title titleComplex of the FimH lectin with a C-linked naphtyl alpha-D-mannoside in soaked trigonal crystals at 2.40 A resolution
Keywords keywordsCELL ADHESION, BACTERIAL ADHESIN, TYPE 1 FIMBRIAE, URINARY TRACT INFECTION, VARIABLE IMMUNOGLOBULIN FOLD; CELL ADHESION
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier22.18
Radius of gyration Rg (electron density) rg_electron21.14
Forward intensity I(0) i019867200.00
Molecular weight molecular_weight34596.0 kDa
Excluded volume excluded_volume43511 ų
Envelope volume envelope_volume49916 ų
Hydration-shell volume shell_volume20242 ų
Envelope diameter envelope_diameter67.9
Shell Rg shell_rg27.07
Envelope Rg envelope_rg21.20
Shape Rg shape_rg21.13
Total Rg total_rg21.96
Total atoms total_atoms4818
Residues n_residues316
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 dmax67.7
Rg (real space) rg_real22.06
Rg uncertainty (real space) rg_real_error0.38
I(0) (real space) i0_real1.9870e+07
I(0) uncertainty (real space) i0_real_error2.4920e+05
Rg (reciprocal space) rg_reciprocal22.09
I(0) (reciprocal space) i0_reciprocal19870000.0000
Solution quality estimate total_estimate0.9150
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary28.3
Skewness Skewness skewness0.097
Kurtosis Kurtosis kurtosis-0.699
Angular range angular_range— – 0.3600 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha3797000.0000
Real-space data points n_real_points68
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.964; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.998; Smooth: 0.999

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd5abza_
Class classb — All beta proteins
Fold Fold foldb.2 — Common fold of diphtheria toxin/transcription factors/cytochrome f
Superfamily Superfamily superfamilyb.2.3 — Bacterial adhesins
Family Family familyb.2.3.2 — Pilus subunits
Domain ID domain_idd5abzb_
Class classb — All beta proteins
Fold Fold foldb.2 — Common fold of diphtheria toxin/transcription factors/cytochrome f
Superfamily Superfamily superfamilyb.2.3 — Bacterial adhesins
Family Family familyb.2.3.2 — Pilus subunits

CATH v4.4 (2 domains)

Domain ID domain_id5abzA00
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily1090 — Fimbrial-type adhesion domain
Domain ID domain_id5abzB00
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily1090 — Fimbrial-type adhesion domain

8. Citations (1)

9. Files and Curves (10)