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2jty

Self-complemented variant of FimA, the main subunit of type 1 pilus

Method: SOLUTION NMR Dmax: 67.7 Å Quality: REASONABLE
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1. Protein Identity and Related Structures Protein Identity & Related Structures

Type-1 fimbrial protein, A chain

Escherichia coli

UniProt P04128

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 24–182 Chain A； UniProt 24–42 Fragment：Fusion protein of Type-1 fimbrial protein and type-1 fimbrial protein No other associated polymer SOLUTION NMR NMR measurement conditions：pH 7；298 K；Ionic strength (raw mmCIF value) 18；Pressure ambient NMR sample composition：1.7 mM [U-98% 13C; U-98% 15N] FimA, 50 M H2O, 5 M D2O, 95% H2O/5% D2O | 95% H2O/5% D2O Resolution not provided

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 2JTY Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
2M5G Solution structure of FimA wt Deposited 2013-02-24 Different construct Different mutation/modification Different experimental conditions Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 24–182（159 aa）
Not recorded No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 7；298 K；Ionic strength (raw mmCIF value) 0.08；Pressure ambient
NMR sample composition 2 mM [U-99% 13C; U-99% 15N] FimA-1, 90% H2O/10% D2O | 90% H2O/10% D2O
Resolution not provided
3SQB Structure of the major type 1 pilus subunit FimA bound to the FimC chaperone Deposited 2011-07-05 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain B 37–182（146 aa） Fragment：UNP residues 37-182
Not recorded PEG DI(HYDROXYETHYL)ETHER × 3 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 5.5；277 K；0.1 M sodium acetate, 0.2 M magnesium chloride, 13% PEG 4000, pH 5.5, VAPOR DIFFUSION, SITTING DROP, temperature 277K
Resolution 3.20 Å R-free 0.300
3SQB Structure of the major type 1 pilus subunit FimA bound to the FimC chaperone Deposited 2011-07-05 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain D 37–182（146 aa） Fragment：UNP residues 37-182
Not recorded EDO 1,2-ETHANEDIOL × 2 TRS 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 5.5；277 K；0.1 M sodium acetate, 0.2 M magnesium chloride, 13% PEG 4000, pH 5.5, VAPOR DIFFUSION, SITTING DROP, temperature 277K
Resolution 3.20 Å R-free 0.300
3SQB Structure of the major type 1 pilus subunit FimA bound to the FimC chaperone Deposited 2011-07-05 Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 3 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain F 37–182（146 aa） Fragment：UNP residues 37-182
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 5.5；277 K；0.1 M sodium acetate, 0.2 M magnesium chloride, 13% PEG 4000, pH 5.5, VAPOR DIFFUSION, SITTING DROP, temperature 277K
Resolution 3.20 Å R-free 0.300
3SQB Structure of the major type 1 pilus subunit FimA bound to the FimC chaperone Deposited 2011-07-05 Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 4 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain H 37–182（146 aa） Fragment：UNP residues 37-182
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 5.5；277 K；0.1 M sodium acetate, 0.2 M magnesium chloride, 13% PEG 4000, pH 5.5, VAPOR DIFFUSION, SITTING DROP, temperature 277K
Resolution 3.20 Å R-free 0.300
4DWH Structure of the major type 1 pilus subunit FIMA bound to the FIMC (2.5 A resolution) Deposited 2012-02-24 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain B 41–182（142 aa）
Not recorded PEG DI(HYDROXYETHYL)ETHER × 7 PG4 TETRAETHYLENE GLYCOL × 1 PO4 PHOSPHATE ION × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；40% (v/v) PEG 400 0.1 M phosphate/citrate pH 4.2 , VAPOR DIFFUSION, SITTING DROP, temperature 293K
Resolution 2.50 Å R-free 0.294
4DWH Structure of the major type 1 pilus subunit FIMA bound to the FIMC (2.5 A resolution) Deposited 2012-02-24 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain D 41–182（142 aa）
Not recorded PEG DI(HYDROXYETHYL)ETHER × 3 PG4 TETRAETHYLENE GLYCOL × 1 PGE TRIETHYLENE GLYCOL × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；40% (v/v) PEG 400 0.1 M phosphate/citrate pH 4.2 , VAPOR DIFFUSION, SITTING DROP, temperature 293K
Resolution 2.50 Å R-free 0.294
5NKT FimA wt from E. coli Deposited 2017-04-03 Different construct Different mutation/modification 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 24–182（159 aa）
Not recorded SO4 SULFATE ION × 4 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 2.6；277 K；0.1 M Sodium Malonate, pH 2.6, 45% ammonium sulphate, 23 mg/ml of protein 1:1 mixture with reservoir
Resolution 1.50 Å R-free 0.188
5OH0 The Cryo-Electron Microscopy Structure of the Type 1 Chaperone-Usher Pilus Rod Deposited 2017-07-13 Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 6 PDB declaration: hexameric
Chain A 24–182（159 aa）
Chain B 24–182（159 aa）
Chain C 24–182（159 aa）
Chain D 24–182（159 aa）
Chain E 24–182（159 aa）
Chain F 24–182（159 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7.5
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 4.20 Å
6C53 Cryo-EM structure of the Type 1 pilus rod Deposited 2018-01-13 Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 11 PDB declaration: undecameric
Chain A 24–182（159 aa）
Chain B 24–182（159 aa）
Chain C 24–182（159 aa）
Chain D 24–182（159 aa）
Chain E 24–182（159 aa）
Chain F 24–182（159 aa）
Chain G 24–182（159 aa）
Chain H 24–182（159 aa）
Chain I 24–182（159 aa）
Chain J 24–182（159 aa）
Chain K 24–182（159 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7.4
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 4.20 Å
6R74 N-terminally reversed variant of FimA E. coli Deposited 2019-03-28 Different construct Different mutation/modification 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 42–182（141 aa）
Not recorded SO4 SULFATE ION × 5 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 3.1；298 K；45% NH4SO2 and 0.1M Sodium Malonate buffer pH 3.1
Resolution 1.81 Å R-free 0.219
6SWH Crystal structure of the ternary complex between the type 1 pilus proteins FimC, FimI and FimA from E. coli Deposited 2019-09-20 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric
Chain C 37–182（146 aa）
Not recorded PEG DI(HYDROXYETHYL)ETHER × 1 EDO 1,2-ETHANEDIOL × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION；293 K；0.8 M sodium formate, 100 mM Tris/acetic acid pH 8.5, 16% PEG 4000 (w/v)
Resolution 2.80 Å R-free 0.207
6SWH Crystal structure of the ternary complex between the type 1 pilus proteins FimC, FimI and FimA from E. coli Deposited 2019-09-20 Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 2 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric
Chain F 37–182（146 aa）
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION；293 K；0.8 M sodium formate, 100 mM Tris/acetic acid pH 8.5, 16% PEG 4000 (w/v)
Resolution 2.80 Å R-free 0.207
6Y7S 2.85 A cryo-EM structure of the in vivo assembled type 1 pilus rod Deposited 2020-03-02 Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 6 PDB declaration: hexameric
Chain A 1–182（182 aa）
Chain B 1–182（182 aa）
Chain C 1–182（182 aa）
Chain D 1–182（182 aa）
Chain E 1–182（182 aa）
Chain F 1–182（182 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7；in ddH2O.
cryo-EM vitrification conditions Cryogen ETHANE；3 ul sample, 30 s wait time, 0.5 s drain time, 6 s blotting
Resolution 2.85 Å R-free 0.275
8PSV 2.7 A cryo-EM structure of in vitro assembled type 1 pilus rod Deposited 2023-07-13 Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 6 PDB declaration: hexameric
Chain A 1–182（182 aa）
Chain B 1–182（182 aa）
Chain C 1–182（182 aa）
Chain D 1–182（182 aa）
Chain E 1–182（182 aa）
Chain F 1–182（182 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7；in ddH2O.
cryo-EM vitrification conditions Cryogen ETHANE；3 ul sample, 30 s wait time, 0.5 s drain time, 6 s blotting
Resolution 2.70 Å
8PTU 2.5 A cryo-EM structure of the in vitro FimD-catalyzed assembly of type 1 pilus rod Deposited 2023-07-14 Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 6 PDB declaration: hexameric
Chain A 1–182（182 aa）
Chain B 1–182（182 aa）
Chain C 1–182（182 aa）
Chain D 1–182（182 aa）
Chain E 1–182（182 aa）
Chain F 1–182（182 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7；in ddH2O.
cryo-EM vitrification conditions Cryogen ETHANE；3 ul sample, 30 s wait time, 0.5 s drain time, 6 s blotting
Resolution 2.52 Å
9FTT Cryo-EM structure of the type 1 pilus rod as part of the FimA-bound usher complex (FimDHGFAnC) Deposited 2024-06-25 Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 10 PDB declaration: decameric
Chain B 24–182（159 aa）
Chain C 24–182（159 aa）
Chain D 24–182（159 aa）
Chain E 24–182（159 aa）
Chain F 24–182（159 aa）
Chain G 24–182（159 aa）
Chain H 24–182（159 aa）
Chain I 24–182（159 aa）
Chain J 24–182（159 aa）
Chain K 24–182（159 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 8
cryo-EM vitrification conditions Cryogen ETHANE-PROPANE
Resolution 3.60 Å
9FW9 Cryo-EM structure of the type 1 pilus assembly platform as part of the FimA-bound chaperone-usher pilus complex (FimDHGFAnC - body 2) Deposited 2024-06-28 Different construct Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric
Chain A 24–182（159 aa）
Chain B 24–182（159 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 8
cryo-EM vitrification conditions Cryogen ETHANE-PROPANE
Resolution 3.90 Å
9FWB Cryo-EM structure of the type 1 pilus assembly platform as part of the FimA-bound chaperone-usher pilus complex (Local refinement including FimD, FimC, FimAn and FimAn-1) Deposited 2024-06-28 Different construct Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric
Chain A 24–182（159 aa）
Chain B 24–182（159 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 8
cryo-EM vitrification conditions Cryogen ETHANE-PROPANE
Resolution 3.50 Å
9FWZ Cryo-EM structure of the type 1 pilus assembly platform as part of the FimA-bound chaperone-usher pilus complex (Local refinement including FimD, FimC, FimAn, FimAn-1 and FimAn-2) Deposited 2024-07-01 Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 5 PDB declaration: pentameric
Chain A 24–182（159 aa）
Chain B 24–182（159 aa）
Chain E 24–182（159 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 8
cryo-EM vitrification conditions Cryogen ETHANE-PROPANE
Resolution 3.60 Å
9FX0 Cryo-EM structure of the type 1 pilus tip-to-rod transition Deposited 2024-07-01 Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 7 PDB declaration: heptameric
Chain A 24–182（159 aa）
Chain B 24–182（159 aa）
Chain C 24–182（159 aa）
Chain D 24–182（159 aa）
Chain E 24–182（159 aa）
Chain G 24–182（159 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 8
cryo-EM vitrification conditions Cryogen ETHANE-PROPANE
Resolution 3.10 Å
9FXA Cryo-EM structure of the type 1 pilus rod as part of the FimI-bound usher complex (FimDHGFAnIC - body 1) Deposited 2024-07-01 Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 10 PDB declaration: decameric
Chain B 24–182（159 aa）
Chain C 24–182（159 aa）
Chain D 24–182（159 aa）
Chain E 24–182（159 aa）
Chain F 24–182（159 aa）
Chain G 24–182（159 aa）
Chain H 24–182（159 aa）
Chain I 24–182（159 aa）
Chain J 24–182（159 aa）
Chain K 24–182（159 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 8
cryo-EM vitrification conditions Cryogen ETHANE-PROPANE
Resolution 4.00 Å
9FXB Cryo-EM structure of the type 1 pilus assembly platform as part of the FimI-bound chaperone-usher pilus complex (FimDHGFAnIC - body 2) Deposited 2024-07-01 Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric
Chain A 24–182（159 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 8
cryo-EM vitrification conditions Cryogen ETHANE-PROPANE
Resolution 4.30 Å
9VKV Cryo-EM structure of the type I pilus from Escherichia Coli and the surrounding water network Deposited 2025-06-24 Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 15 PDB declaration: pentadecameric
Chain A 24–182（159 aa）
Chain B 24–182（159 aa）
Chain C 24–182（159 aa）
Chain D 24–182（159 aa）
Chain E 24–182（159 aa）
Chain F 24–182（159 aa）
Chain G 24–182（159 aa）
Chain H 24–182（159 aa）
Chain I 24–182（159 aa）
Chain J 24–182（159 aa）
Chain K 24–182（159 aa）
Chain L 24–182（159 aa）
Chain M 24–182（159 aa）
Chain N 24–182（159 aa）
Chain O 24–182（159 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7.5
cryo-EM vitrification conditions Cryogen NITROGEN
Resolution 2.09 Å
9X67 Cryo-EM structure of the type I pilus from Escherichia Coli and the surrounding water network Deposited 2025-10-15 Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 15 PDB declaration: 15-meric
Chain A 24–182（159 aa）
Chain B 24–182（159 aa）
Chain C 24–182（159 aa）
Chain D 24–182（159 aa）
Chain E 24–182（159 aa）
Chain F 24–182（159 aa）
Chain G 24–182（159 aa）
Chain H 24–182（159 aa）
Chain I 24–182（159 aa）
Chain J 24–182（159 aa）
Chain K 24–182（159 aa）
Chain L 24–182（159 aa）
Chain M 24–182（159 aa）
Chain N 24–182（159 aa）
Chain O 24–182（159 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7.5
cryo-EM vitrification conditions Cryogen NITROGEN
Resolution 1.85 Å

20 other PDB entries and 25 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name FIMA1_ECOLI
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A； PDBConstruct 1–159； UniProt 24–182 Author chain A； PDBConstruct 166–184； UniProt 24–42

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 2jty

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id2jty
Deposition date deposition_date2007-08-09
Structure title titleSelf-complemented variant of FimA, the main subunit of type 1 pilus
Keywords keywordsPROTEIN/PILI/FIM, Cell projection, Fimbrium, chimera, CHAPERONE, STRUCTURAL PROTEIN; STRUCTURAL PROTEIN
Experimental Method methodSOLUTION NMR
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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier17.93 Å
Radius of gyration Rg (electron density) rg_electron17.53 Å
Forward intensity I(0) i02033940000.00
Molecular weight molecular_weight360030.0 kDa
Excluded volume excluded_volume441350 ų
Envelope volume envelope_volume50723 ų
Hydration-shell volume shell_volume19803 ų
Envelope diameter envelope_diameter77.1 Å
Shell Rg shell_rg28.72 Å
Envelope Rg envelope_rg23.62 Å
Shape Rg shape_rg17.51 Å
Total Rg total_rg17.78 Å
Total atoms total_atoms49780
Residues n_residues3680
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 Å−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
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4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax67.7 Å
Rg (real space) rg_real18.06 Å
Rg uncertainty (real space) rg_real_error0.74 Å
I(0) (real space) i0_real2.0340e+09
I(0) uncertainty (real space) i0_real_error2.6160e+07
Rg (reciprocal space) rg_reciprocal18.04 Å
I(0) (reciprocal space) i0_reciprocal2034000000.0000
Solution quality estimate total_estimate0.7014
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary18.3 Å
Skewness Skewness skewness0.532
Kurtosis Kurtosis kurtosis-0.105
Angular range angular_range— – 0.4450 Å−1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha1197000.0000
Real-space data points n_real_points75
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.462; Stabil: 0.998; Sysdev: 1.000; Positv: 1.000; Valcen: 0.732; Smooth: 0.000
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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (1)

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7. Fold Classification (SCOP + CATH) 1 domains

CATH v4.4 (1 domains)

Domain ID domain_id2jtyA00
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily1090 — Fimbrial-type adhesion domain
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8. Citations (1)

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9. Files and Curves (10)