← Back to search
4x69

Crystal structure of OP0595 complexed with CTX-M-44

Method: X-RAY DIFFRACTION Dmax: 78.6 Å Quality: EXCELLENT
▼

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

Beta-lactamase Toho-1

Escherichia coli

UniProt Q47066

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 30–291 Not recorded OP0 (2S,5R)-N-(2-aminoethoxy)-1-formyl-5-[(sulfooxy)amino]piperidine-2-carboxamide × 1 EDO 1,2-ETHANEDIOL × 1 X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION；pH 8；293 K；PEG 6000 Resolution 1.42 Å R-free 0.208
2 Protein monomer Monomer Protein × 1 PDB declaration: monomeric（1） Consistent with protein copy count Chain B； UniProt 30–291 Not recorded OP0 (2S,5R)-N-(2-aminoethoxy)-1-formyl-5-[(sulfooxy)amino]piperidine-2-carboxamide × 1 EDO 1,2-ETHANEDIOL × 1 X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION；pH 8；293 K；PEG 6000 Resolution 1.42 Å R-free 0.208

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 4X69 Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
1BZA BETA-LACTAMASE TOHO-1 FROM ESCHERICHIA COLI TUH12191 Deposited 1998-10-28 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 33–290（258 aa）
Mutation：E166A SO4 SULFATE ION × 2 X-RAY DIFFRACTION
X-ray crystallization conditions pH 4.5；pH 4.5
Resolution 1.80 Å R-free 0.217
1IYO Toho-1 beta-Lactamase In Complex With Cefotaxime Deposited 2002-09-04 Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 30–291（262 aa）
Mutation：E166A SO4 SULFATE ION × 3 CEF CEFOTAXIME, C3' cleaved, open, bound form × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；300 K；ammonium sulfate, VAPOR DIFFUSION, HANGING DROP, temperature 300K
Resolution 1.80 Å R-free 0.206
1IYP Toho-1 beta-Lactamase In Complex With Cephalothin Deposited 2002-09-04 Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 30–291（262 aa）
Mutation：E166A SO4 SULFATE ION × 3 CEP CEPHALOTHIN GROUP × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；300 K；ammonium sulfate, VAPOR DIFFUSION, HANGING DROP, temperature 300K
Resolution 2.00 Å R-free 0.245
1IYQ Toho-1 beta-Lactamase In Complex With Benzylpenicillin Deposited 2002-09-04 Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 30–291（262 aa）
Mutation：E166A SO4 SULFATE ION × 3 PNM OPEN FORM - PENICILLIN G × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；300 K；ammonium sulfate, VAPOR DIFFUSION, HANGING DROP, temperature 300K
Resolution 2.10 Å R-free 0.227
1IYS Crystal Structure of Class A beta-Lactamase Toho-1 Deposited 2002-09-06 Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 31–291（261 aa）
Not recorded SO4 SULFATE ION × 8 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6；298 K；ammonium sulfate, sodium acetate, acetate, pH 6.0, VAPOR DIFFUSION, HANGING DROP, temperature 298.0K
Resolution 1.65 Å R-free 0.197
1WE4 Crystal Structure of Class A beta-Lactamase Toho-1 G238C mutant Deposited 2004-05-24 Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 30–291（262 aa）
Mutation：A26M, G238C SO4 SULFATE ION × 7 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6；298 K；Ammonium sulfate, sodium acetate, pH 6.0, VAPOR DIFFUSION, HANGING DROP, temperature 298K
Resolution 1.70 Å R-free 0.222
2WYX Neutron structure of a class A Beta-lactamase Toho-1 E166A R274N R276N triple mutant Deposited 2009-11-20 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 33–288（256 aa） Fragment：RESIDUES 33-288
Mutation：YES No recorded non-water small molecule NEUTRON DIFFRACTION
X-ray crystallization conditions pH 6.5；pH 6.5
Resolution 2.10 Å R-free 0.258
2XQZ Neutron structure of the perdeuterated Toho-1 R274N R276N double mutant beta-lactamase Deposited 2010-09-08 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 32–291（260 aa） Fragment：RESIDUES 32-291
Mutation：YES No recorded non-water small molecule NEUTRON DIFFRACTION
X-ray crystallization conditions pH 6.5；pH 6.5
Resolution 2.10 Å R-free 0.259
2XR0 Room temperature X-ray structure of the perdeuterated Toho-1 R274N R276N double mutant beta-lactamase Deposited 2010-09-08 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 32–291（260 aa） Fragment：RESIDUES 32-291
Mutation：YES SO4 SULFATE ION × 3 X-RAY DIFFRACTION
X-ray crystallization conditions pH 6.5；2.0 A AMMONIUM SULFATE, 0.1 M SODIUM CITRATE, PD 5.1. PREPARED IN 99.9% D2O AND MIXED 1:1 WITH PERDEUTERATED PROTEIN PREPARED IN 20 MM NA MES AT PD 6.1 (PH 6.5).
Resolution 2.20 Å R-free 0.173
2ZQ7 Apo structure of Class A beta-lactamase Toho-1 E166A/R274N/R276N triple mutant Deposited 2008-08-07 Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 30–291（262 aa）
Mutation：E166A, R274N, R276N SO4 SULFATE ION × 5 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5.5；298 K；1.95-2.10M Ammonium sulfate, 0.2M sodium citrate, pH5.50, VAPOR DIFFUSION, HANGING DROP, temperature 298K
Resolution 0.94 Å R-free 0.147
2ZQ8 Apo structure of class a beta-lactamase Toho-1 R274N/R276N double mutant Deposited 2008-08-07 Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 30–291（262 aa）
Mutation：R274N, R276N SO4 SULFATE ION × 5 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5.5；298 K；1.95-2.10M ammonium sulfate, 0.2M sodium citrate, PH5.50, VAPOR DIFFUSION, HANGING DROP, temperature 298K
Resolution 1.03 Å R-free 0.148
2ZQ9 Cephalothin acyl-intermediate structure of class a beta-lactamase Toho-1 E166A/R274N/R276N triple mutant Deposited 2008-08-07 Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 30–291（262 aa）
Mutation：E166A, R274N, R276N SO4 SULFATE ION × 2 CEO 5-METHYLENE-2-[2-OXO-1-(2-THIOPHEN-2-YL-ACETYLAMINO)-ETHYL]-5,6-DIHYDRO-2H-[1,3]THIAZINE-4-CARBOXYLIC ACID × 1 CLS CEPHALOTHIN × 1 SPA THIOPHENEACETIC ACID × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5.5；298 K；1.95-2.10M ammonium sulfate, 0.2M sodium citrate, PH5.50, VAPOR DIFFUSION, HANGING DROP, temperature 298K
Resolution 1.07 Å R-free 0.146
2ZQA Cefotaxime acyl-intermediate structure of class a beta-lacta Toho-1 E166A/R274N/R276N triple mutant Deposited 2008-08-07 Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 30–291（262 aa）
Mutation：E166A, R274N, R276N CEF CEFOTAXIME, C3' cleaved, open, bound form × 1 SO4 SULFATE ION × 4 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5.5；298 K；1.95-2.10M ammonium sulfate, 0.2M sodium citrate, PH5.50, VAPOR DIFFUSION, HANGING DROP, temperature 298K
Resolution 0.95 Å R-free 0.145
2ZQC Aztreonam acyl-intermediate structure of class a beta-lactam Toho-1 E166A/R274N/R276N triple mutant Deposited 2008-08-07 Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 30–291（262 aa）
Mutation：E166A, R274N, R276N SO4 SULFATE ION × 4 AZR 2-({[(1Z)-1-(2-amino-1,3-thiazol-4-yl)-2-oxo-2-{[(2S,3S)-1-oxo-3-(sulfoamino)butan-2-yl]amino}ethylidene]amino}oxy)-2-methylpropanoic acid × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5.5；298 K；1.95-2.10M ammonium sulfate, 0.2M sodium citrate, PH5.50, VAPOR DIFFUSION, HANGING DROP, temperature 298K
Resolution 1.07 Å R-free 0.146
2ZQD Ceftazidime acyl-intermediate structure of class a beta-lact Toho-1 E166A/R274N/R276N triple mutant Deposited 2008-08-07 Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 30–291（262 aa）
Mutation：E166A, R274N, R276N SO4 SULFATE ION × 4 CAZ ACYLATED CEFTAZIDIME × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5.5；298 K；1.95-2.10M Ammonium sulfate, 0.2M sodium citrate, PH5.50, VAPOR DIFFUSION, HANGING DROP, temperature 298K
Resolution 1.19 Å R-free 0.159
4BD0 X-ray structure of a perdeuterated Toho-1 R274N R276N double mutant Beta-lactamase in complex with a fully deuterated boronic acid (BZB) Deposited 2012-10-04 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 31–291（261 aa） Fragment：RESIDUES 32-291
Mutation：YES BZB BENZO[B]THIOPHENE-2-BORONIC ACID × 1 SO4 SULFATE ION × 6 X-RAY DIFFRACTION
X-ray crystallization conditions 293 K；2.0 M AMMONIUM SULFATE AND 0.1 M SODIUM CITRATE PD 5.1 PREPARED IN 99.9 PERCENT D2O AT 20 C
Resolution 1.21 Å R-free 0.133
4BD1 Neutron structure of a perdeuterated Toho-1 R274N R276N double mutant Beta-lactamase in complex with a fully deuterated boronic acid (BZB) Deposited 2012-10-04 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 31–291（261 aa）
Mutation：YES BZB BENZO[B]THIOPHENE-2-BORONIC ACID × 1 NEUTRON DIFFRACTION
X-ray crystallization conditions pH 6.5；PH 6.5
Resolution 2.00 Å R-free 0.257
4C3Q Neutron structure of a perdeuterated Toho-1 R274N R276N double mutant Beta-lactamase in complex with a fully deuterated boronic acid (BZB) at 100K Deposited 2013-08-26 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 31–291（261 aa）
Mutation：YES BZB BENZO[B]THIOPHENE-2-BORONIC ACID × 1 NEUTRON DIFFRACTION
X-ray crystallization conditions pH 5.6；PH 5.6
Resolution 2.20 Å R-free 0.240
5A91 15K X-ray ligand free: Exploring the Mechanism of beta-Lactam Ring Protonation in the Class A beta-lactamase Acylation Mechanism Using Neutron and X-ray Crystallography Deposited 2015-07-17 Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 30–291（262 aa）
Mutation：YES SO4 SULFATE ION × 5 X-RAY DIFFRACTION
X-ray crystallization conditions 293 K；300 ul of a 10 mg/ml protein concentration in a solution containing 2.0 M ammonium sulfate and 0.1 M sodium citrate (pH 6.1) prepared in D 2 O.
Resolution 1.20 Å R-free 0.150
5KMW TOHO1 Beta lactamase mutant E166A/R274N/R276N -benzyl penicillin complex Deposited 2016-06-27 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 33–288（256 aa）
Mutation：E165A, R271N, R273N SO4 SULFATE ION × 5 PNM OPEN FORM - PENICILLIN G × 1 PNN PENICILLIN G × 2 X-RAY DIFFRACTION
X-ray crystallization conditions BATCH MODE；pH 6.1；293.15 K；30 microliters of 10 mg/ml protein concentration was added to a solution containing 2.0 M ammonium sulfate and 0.1 M sodium citrate (pH 6.1). For ligand soaking, crystals were placed for 2-3 h in a reservoir solution containing 2.7 M ammonium sulfate, 0.1 M sodium citrate (pH 6.1), and 5.0 mM benzyl penicillin. The crystals were then placed momentarily in a reservoir solution containing a cryoprotectant (30% w/v trehalose) and subsequently flash-frozen in liquid nitrogen
Resolution 1.10 Å R-free 0.170
5KSC E166A/R274N/R276N Toho-1 Beta-lactamase aztreonam acyl-enzyme intermediate Deposited 2016-07-08 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 31–291（261 aa）
Mutation：E169A, R275N, R277N AZR 2-({[(1Z)-1-(2-amino-1,3-thiazol-4-yl)-2-oxo-2-{[(2S,3S)-1-oxo-3-(sulfoamino)butan-2-yl]amino}ethylidene]amino}oxy)-2-methylpropanoic acid × 1 NEUTRON DIFFRACTION
X-ray crystallization conditions BATCH MODE；pH 6.1；293.15 K；300 microliters of a 10 mg/ml protein concentration in a solution containing 2.0 M ammonium sulfate and 0.1 M sodium citrate (pH 6.1) prepared in D2O.
Resolution 2.10 Å R-free 0.280
6C78 Substrate Binding Induces Conformational Changes In A Class A Beta Lactamase That Primes It For Catalysis Deposited 2018-01-22 Different construct 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 32–291（260 aa） Fragment：RESIDUES 32-291
Not recorded No recorded non-water small molecule NEUTRON DIFFRACTION
X-ray crystallization conditions BATCH MODE；pH 6.1；293 K；300 MICROLITERS OF A 10 MG/ML PROTEIN CONCENTRATION IN A SOLUTION CONTAINING 2.0 M AMMONIUM SULFATE AND 0.1 M PREPARED IN D2O, PH 6.1, BATCH MODE, TEMPERATURE 293K
Resolution 1.75 Å
6C79 Conformational Changes in a Class A Beta lactamase that Prime it for Catalysis Deposited 2018-01-22 Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 32–291（260 aa） Fragment：residues 32-291
Not recorded CE3 (6R,7R)-3-(acetyloxymethyl)-7-[[(2Z)-2-(2-amino-1,3-thiazol-4-yl)-2-methoxyimino-ethanoyl]amino]-8-oxo-5-thia-1-azabicy clo[4.2.0]oct-2-ene-2-carboxylic acid × 1 SO4 SULFATE ION × 4 X-RAY DIFFRACTION
X-ray crystallization conditions BATCH MODE；pH 6.1；293 K；10 mg/ml protein in a solution containing 2.0 M ammonium sulfate and 0.1 M sodium citrate (pH 6.1)
Resolution 1.10 Å R-free 0.164
6C7A Conformational Changes in a Class A Beta lactamase that Prime it for Catalysis Deposited 2018-01-22 Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 32–291（260 aa） Fragment：residues 32-291
Not recorded SO4 SULFATE ION × 9 X-RAY DIFFRACTION
X-ray crystallization conditions BATCH MODE；pH 6.1；293 K；10 mg/ml protein in a solution containing 2.0 M ammonium sulfate and 0.1 M sodium citrate (pH 6.1)
Resolution 1.05 Å R-free 0.150

24 other PDB entries and 24 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name BLT1_ECOLX
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A； PDBConstruct 1–262； UniProt 30–291 Author chain B； PDBConstruct 1–262； UniProt 30–291

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 4x69

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 4x69
Download Download
▼

2. Structure Basics 2. Structure Basics

Entry ID entry_id4x69
Deposition date deposition_date2014-12-07
Structure title titleCrystal structure of OP0595 complexed with CTX-M-44
Keywords keywordsHYDROLASE-HYDROLASE INHIBITOR COMPLEX; HYDROLASE/HYDROLASE INHIBITOR
Experimental Method methodX-RAY DIFFRACTION
▼

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

Radius of gyration Rg (Guinier) rg_guinier25.36 Å
Radius of gyration Rg (electron density) rg_electron24.45 Å
Forward intensity I(0) i056227900.00
Molecular weight molecular_weight56973.0 kDa
Excluded volume excluded_volume70878 ų
Envelope volume envelope_volume83834 ų
Hydration-shell volume shell_volume28023 ų
Envelope diameter envelope_diameter79.8 Å
Shell Rg shell_rg31.80 Å
Envelope Rg envelope_rg24.45 Å
Shape Rg shape_rg24.46 Å
Total Rg total_rg25.21 Å
Total atoms total_atoms4000
Residues n_residues522
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
▼

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

Maximum dimension Dmax dmax78.6 Å
Rg (real space) rg_real25.27 Å
Rg uncertainty (real space) rg_real_error0.42 Å
I(0) (real space) i0_real5.6230e+07
I(0) uncertainty (real space) i0_real_error7.7750e+05
Rg (reciprocal space) rg_reciprocal25.30 Å
I(0) (reciprocal space) i0_reciprocal56230000.0000
Solution quality estimate total_estimate0.9115
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary30.0 Å
Skewness Skewness skewness0.173
Kurtosis Kurtosis kurtosis-0.616
Angular range angular_range— – 0.3150 Å−1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha10080000.0000
Real-space data points n_real_points64
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.952; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.999; Smooth: 0.989
▶

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_idd4x69a_
Class classe — Multi-domain proteins (alpha and beta)
Fold Fold folde.3 — beta-lactamase/transpeptidase-like
Superfamily Superfamily superfamilye.3.1 — beta-lactamase/transpeptidase-like
Family Family familye.3.1.1 — beta-Lactamase/D-ala carboxypeptidase
Domain ID domain_idd4x69b_
Class classe — Multi-domain proteins (alpha and beta)
Fold Fold folde.3 — beta-lactamase/transpeptidase-like
Superfamily Superfamily superfamilye.3.1 — beta-lactamase/transpeptidase-like
Family Family familye.3.1.1 — beta-Lactamase/D-ala carboxypeptidase

CATH v4.4 (2 domains)

Domain ID domain_id4x69A00
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology710 — Beta-lactamase
Homologous superfamily homologous superfamily10 — DD-peptidase/beta-lactamase superfamily
Domain ID domain_id4x69B00
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology710 — Beta-lactamase
Homologous superfamily homologous superfamily10 — DD-peptidase/beta-lactamase superfamily
▶

8. Citations (1)

▶

9. Files and Curves (10)