1qak

THE ACTIVE SITE BASE CONTROLS COFACTOR REACTIVITY IN ESCHERICHIA COLI AMINE OXIDASE : X-RAY CRYSTALLOGRAPHIC STUDIES WITH MUTATIONAL VARIANTS

Method: X-RAY DIFFRACTION D_max: 103.8 Å Quality: GOOD

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

COPPER AMINE OXIDASE

Escherichia coli

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 homooligomer Homooligomer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain A； UniProt 36–757 Chain B； UniProt 36–757	Mutation：D383A Non-standard monomer：Yes (specific site not provided by mmCIF)	CU COPPER (II) ION × 2 CA CALCIUM ION × 4	X-RAY DIFFRACTION X-ray crystallization conditions：pH 7.1；pH 7.1	Resolution 2.00 Å R-free 0.244

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 1QAK	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1D6U CRYSTAL STRUCTURE OF E. COLI AMINE OXIDASE ANAEROBICALLY REDUCED WITH BETA-PHENYLETHYLAMINE Deposited 1999-10-15	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 31–757（727 aa） Chain B 31–757（727 aa）	Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF)	CU COPPER (II) ION × 2 CA CALCIUM ION × 4 HY1 PHENYLACETALDEHYDE × 2 PEA 2-PHENYLETHYLAMINE × 1 GOL GLYCEROL × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.2；291 K；SODIUM CITRATE, HEPES BUFFER, pH 7.2, VAPOR DIFFUSION, SITTING DROP, temperature 18K	Resolution 2.40 Å R-free 0.239
1D6Y CRYSTAL STRUCTURE OF E. COLI COPPER-CONTAINING AMINE OXIDASE ANAEROBICALLY REDUCED WITH BETA-PHENYLETHYLAMINE AND COMPLEXED WITH NITRIC OXIDE. Deposited 1999-10-16	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 31–757（727 aa） Chain B 31–757（727 aa）	Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF)	CU COPPER (II) ION × 2 CA CALCIUM ION × 4 HY1 PHENYLACETALDEHYDE × 2 NO NITRIC OXIDE × 2 PEA 2-PHENYLETHYLAMINE × 1 GOL GLYCEROL × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.2；291 K；sodium citrate, HEPES buffer, pH 7.2, VAPOR DIFFUSION, SITTING DROP, temperature 18K	Resolution 2.40 Å R-free 0.231
1D6Z CRYSTAL STRUCTURE OF THE AEROBICALLY FREEZE TRAPPED RATE-DETERMINING CATALYTIC INTERMEDIATE OF E. COLI COPPER-CONTAINING AMINE OXIDASE. Deposited 1999-10-16	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 31–757（727 aa） Chain B 31–757（727 aa）	Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF)	CU COPPER (II) ION × 2 CA CALCIUM ION × 4 HY1 PHENYLACETALDEHYDE × 2 PEO HYDROGEN PEROXIDE × 2 PEA 2-PHENYLETHYLAMINE × 1 GOL GLYCEROL × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.2；291 K；sodium citrate, HEPES buffer, pH 7.2, VAPOR DIFFUSION, SITTING DROP, temperature 18K	Resolution 2.10 Å R-free 0.237
1DYU The active site base controls cofactor reactivity in Escherichia coli amine oxidase: X-ray crystallographic studies with mutational variants. Deposited 2000-02-08	Different construct Different mutation/modification Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 31–757（727 aa） Chain B 31–757（727 aa）	Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF)	CU COPPER (II) ION × 2 CA CALCIUM ION × 4	X-RAY DIFFRACTION X-ray crystallization conditions pH 7.1；1.2 M SODIUM CITRATE, 0.1 M HEPES PH 7.1	Resolution 2.04 Å R-free 0.237
1JRQ X-ray Structure Analysis of the Role of the Conserved Tyrosine-369 in Active Site of E. coli Amine Oxidase Deposited 2001-08-14	Different construct Different mutation/modification Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 31–757（727 aa） Chain B 31–757（727 aa）	Mutation：Y369F Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：Y369F Non-standard monomer：Yes (specific site not provided by mmCIF)	CU COPPER (II) ION × 2 CA CALCIUM ION × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.4；291 K；SODIUM CITRATE, HEPES BUFFER, pH 7.40, VAPOR DIFFUSION, SITTING DROP, temperature 291K	Resolution 2.15 Å R-free 0.235
1LVN CRYSTAL STRUCTURE OF E. COLI AMINE OXIDASE COMPLEXED WITH TRANYLCYPROMINE Deposited 2002-05-28	Different construct Different mutation/modification Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 31–757（727 aa） Chain B 31–757（727 aa）	Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF)	CU COPPER (II) ION × 2 CA CALCIUM ION × 4	X-RAY DIFFRACTION X-ray crystallization conditions Sitting drop；pH 7.2；291 K；1.3M SODIUM CITRATE, 0.1M HEPES BUFFER, pH 7.2, INHIBITOR SOAKING SOLUTION 10:1 RATIO OF RACEMIC TRANYLCYPROMINE TO ENZYME MADE UP IN 1.4M SODIUM CITRATE, 0.1M HEPES BUFFER, PH 7.2. CRYSTAL SOAKED FOR 20 DAYS.CRYOPROTECTANT 20% GLYCEROL, 1.4M SODIUM CITRATE BUFFER, PH 7.2, pH 7.20, Sitting drop, temperature 291.0K	Resolution 2.40 Å R-free 0.229
1OAC CRYSTAL STRUCTURE OF A QUINOENZYME: COPPER AMINE OXIDASE OF ESCHERICHIA COLI AT 2 ANGSTROEMS RESOLUTION Deposited 1995-09-27	Different construct Different mutation/modification Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 31–757（727 aa） Chain B 31–757（727 aa）	Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF)	CU COPPER (II) ION × 2 CA CALCIUM ION × 4	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.00 Å
1QAF THE ACTIVE SITE BASE CONTROLS COFACTOR REACTIVITY IN ESCHERICHIA COLI AMINE OXIDASE : X-RAY CRYSTALLOGRAPHIC STUDIES WITH MUTATIONAL VARIANTS Deposited 1999-03-11	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 36–756（721 aa） Chain B 36–756（721 aa）	Mutation：D383E Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：D383E Non-standard monomer：Yes (specific site not provided by mmCIF)	CU COPPER (II) ION × 2 CA CALCIUM ION × 4 GOL GLYCEROL × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.1；315 K；VAPOR DIFFUSION, SITTING DROP PH 7.1, 315 K SODIUM CITRATE, HEPES	Resolution 2.20 Å R-free 0.244
1QAL THE ACTIVE SITE BASE CONTROLS COFACTOR REACTIVITY IN ESCHERICHIA COLI AMINE OXIDASE : X-RAY CRYSTALLOGRAPHIC STUDIES WITH MUTATIONAL VARIANTS Deposited 1999-03-19	Different construct Different mutation/modification Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 36–756（721 aa） Chain B 36–756（721 aa）	Mutation：D383N Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：D383N Non-standard monomer：Yes (specific site not provided by mmCIF)	CU COPPER (II) ION × 2 CA CALCIUM ION × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.1；315 K；VAPOR DIFFUSION, SITTING DROP, PH 7.1, 315K, 1.2 M SODIUM CITRATE, 0.1 M HEPES CRYOPROTECTANT 1.4 M SODIUM CITRATE 0.1M HEPES 20% GLYCEROL	Resolution 2.20 Å R-free 0.241
1SPU STRUCTURE OF OXIDOREDUCTASE Deposited 1996-11-13	Different construct Different mutation/modification Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 31–757（727 aa） Chain B 31–757（727 aa）	Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF)	CU COPPER (II) ION × 2 CA CALCIUM ION × 4	X-RAY DIFFRACTION X-ray crystallization conditions pH 7.2；1.4M SODIUM CITRATE, 0.1M HEPES BUFFER, PH 7.2 PROTEIN SOLUTION CONCENTRATION 6.5 MG/ML INHIBITOR SOAKING SOLUTION 0.375MM 2-HYDRAZINOPYRIDINE MADE UP IN 1.4M SODIUM CITRATE, 0.1M HEPES BUFFER, PH 7.2. CRYSTAL SOAKED FOR 30 DAYS. CRYOPROTECTANT 20% GLYCEROL, 1.44M SODIUM CITRATE BUFFER, PH 6.4	Resolution 2.00 Å
2W0Q E. coli copper amine oxidase in complex with Xenon Deposited 2008-08-20	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 31–757（727 aa） Chain B 31–757（727 aa）	Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF)	CU COPPER (II) ION × 2 CA CALCIUM ION × 4 XE XENON × 11	X-RAY DIFFRACTION X-ray crystallization conditions pH 7.1；100MM HEPES, PH 7.1, 1.2 M SODIUM CITRATE	Resolution 2.48 Å R-free 0.219
2WGQ Zinc substituted E Coli Copper Amine Oxidase, a model for the precursor for 2,4,5-trihydroxyphenylalaninequinone formation Deposited 2009-04-23	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 31–757（727 aa） Chain B 31–757（727 aa）	Not recorded	ZN ZINC ION × 2 CA CALCIUM ION × 4	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.50 Å R-free 0.264
2WO0 EDTA treated E. coli copper amine oxidase Deposited 2009-07-21	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 31–757（727 aa） Fragment：RESIDUES 31-757 Chain B 31–757（727 aa） Fragment：RESIDUES 31-757	Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF)	CU COPPER (II) ION × 2 NA SODIUM ION × 4	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.60 Å R-free 0.248
2WOF EDTA treated E. coli copper amine oxidase Deposited 2009-07-23	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 31–757（727 aa） Chain B 31–757（727 aa）	Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF)	CU COPPER (II) ION × 2 NA SODIUM ION × 4	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.25 Å R-free 0.220
2WOH Strontium soaked E. coli copper amine oxidase Deposited 2009-07-23	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 31–757（727 aa） Chain B 31–757（727 aa）	Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF)	CU COPPER (II) ION × 2 CA CALCIUM ION × 2 SR STRONTIUM ION × 2	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.70 Å R-free 0.243
6EZZ Crystal structure of Escherichia coli amine oxidase mutant E573Q Deposited 2017-11-16	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 31–757（727 aa） Chain B 31–757（727 aa）	Mutation：E573Q Mutation：E573Q	CU COPPER (II) ION × 2 CA CALCIUM ION × 2 GOL GLYCEROL × 9	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；291.15 K；1.6 M Sodium citrate, 100mM HEPES pH 6-7	Resolution 1.80 Å R-free 0.197

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

View Construct and Data Evidence

UniProt name	AMO_ECOLI
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–722； UniProt 36–757 Author chain B； PDBConstruct 1–722； UniProt 36–757

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

P(r) Distance Distribution P(r) Distribution

Download Download SAXS (.dat) P(r) (.pr.out) CIF

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2. Structure Basics 2. Structure Basics

Entry ID entry_id	1qak
Deposition date deposition_date	1999-03-15
Structure title title	THE ACTIVE SITE BASE CONTROLS COFACTOR REACTIVITY IN ESCHERICHIA COLI AMINE OXIDASE : X-RAY CRYSTALLOGRAPHIC STUDIES WITH MUTATIONAL VARIANTS
Keywords keywords	OXIDOREDUCTASE, COPPER, TPQ, PERIPLASMIC, CATALYTIC BASE MUTANT; OXIDOREDUCTASE
Experimental Method method	X-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier	33.81 Å
Radius of gyration Rg (electron density) rg_electron	33.11 Å
Forward intensity I(0) i0	395802000.00
Molecular weight molecular_weight	161430.0 kDa
Excluded volume excluded_volume	202020 Å³
Envelope volume envelope_volume	242310 Å³
Hydration-shell volume shell_volume	57915 Å³
Envelope diameter envelope_diameter	114.0 Å
Shell Rg shell_rg	42.07 Å
Envelope Rg envelope_rg	33.34 Å
Shape Rg shape_rg	33.08 Å
Total Rg total_rg	33.82 Å
Total atoms total_atoms	11376
Residues n_residues	1440
Spherical-harmonic order n_harmonics	20
q range q_range	— – 0.5000 Å⁻¹
Data points n_points	101
Shell type shell_type	directional
Solvent electron density solvent_density	0.3340 e/Å³
Shell contrast contrast_shell	0.0300 e/Å³
CRYSOL version crysol_version	4.1.3

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

Maximum dimension Dmax dmax	103.8 Å
Rg (real space) rg_real	33.64 Å
Rg uncertainty (real space) rg_real_error	0.68 Å
I(0) (real space) i0_real	3.9580e+08
I(0) uncertainty (real space) i0_real_error	6.2450e+06
Rg (reciprocal space) rg_reciprocal	33.75 Å
I(0) (reciprocal space) i0_reciprocal	395800000.0000
Solution quality estimate total_estimate	0.8970
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	42.0 Å
Skewness Skewness skewness	0.178
Kurtosis Kurtosis kurtosis	-0.435
Angular range angular_range	— – 0.2350 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	105800000.0000
Real-space data points n_real_points	48
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.924; Stabil: 0.998; Sysdev: 1.000; Positv: 1.000; Valcen: 0.985; Smooth: 0.906

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (4)

Entity 1 Entity 1 polymer

Description description	COPPER AMINE OXIDASE
Molecular weight formula_weight	80870.3 kDa
EC 编号 ec_number	1.4.3.4
Mutation mutation	D383A
Source method src_method	man
Copy count entity_count	2

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B
Atom count atom_count	12895

HMVPMDKTLKEFGADVQWDDYAQLFTLIKDGAYVKVKPGAQTAIVNGQPLALQVPVVMKDNKAWVSDTFINDVFQSGLDQTFQVEKRPHPLNALTADEIKQAVEIVKASADFKPNTRFTEISLLPPDKEAVWAFALENKPVDQPRKADVIMLDGKHIIEAVVDLQNNKLLSWQPIKDAHGMVLLDDFASVQNIINNSEEFAAAVKKRGITDAKKVITTPLTVGYFDGKDGLKQDARLLKVISYLDVGDGNYWAHPIENLVAVVDLEQKKIVKIEEGPVVPVPMTARPFDGRDRVAPAVKPMQIIEPEGKNYTITGDMIHWRNWDFHLSMNSRVGPMISTVTYNDNGTKRKVMYEGSLGGMIVPYGDPDIGWYFKAYLASGDYGMGTLTSPIARGKDAPSNAVLLNETIADYTGVPMEIPRAIAVFERYAGPEYKHQEMGQPNVSTERRELVVRWISTVGNYDYIFDWIFHENGTIGIDAGATGIEAVKGVKAKTMHDETAKDDTRYGTLIDHNIVGTTHQHIYNFRLDLDVDGENNSLVAMDPVVKPNTAGGPRTSTMQVNQYNIGNEQDAAQKFDPGTIRLLSNPNKENRMGNPVSYQIIPYAGGTHPVAKGAQFAPDEWIYHRLSFMDKQLWVTRYHPGERFPEGKYPNRSTHDTGLGQYSKDNESLDNTDAVVWMTTGTTHVARAEEWPIMPTEWVHTLLKPWNFFDETPTLGALKKDK

来源 Source

来源生物 organism	Escherichia coli
NCBI Class编号 ncbi_taxonomy_id	562
宿主生物 host_organism	Escherichia coli

Entity 2 Entity 2 non-polymer

Description description	COPPER (II) ION
Molecular weight formula_weight	63.5 kDa
Source method src_method	syn
Copy count entity_count	2

Entity 3 Entity 3 non-polymer

Description description	CALCIUM ION
Molecular weight formula_weight	40.1 kDa
Source method src_method	syn
Copy count entity_count	4

Entity 4 Entity 4 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	1491

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7. Fold Classification (SCOP + CATH) 16 domains

SCOP 2.08 (8 domains)

Domain ID domain_id	d1qaka1
Class class	b — All beta proteins
Fold Fold fold	b.30 — Supersandwich
Superfamily Superfamily superfamily	b.30.2 — Amine oxidase catalytic domain
Family Family family	b.30.2.1 — Amine oxidase catalytic domain

Domain ID domain_id	d1qaka2
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.17 — Cystatin-like
Superfamily Superfamily superfamily	d.17.2 — Amine oxidase N-terminal region
Family Family family	d.17.2.1 — Amine oxidase N-terminal region

Domain ID domain_id	d1qaka3
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.17 — Cystatin-like
Superfamily Superfamily superfamily	d.17.2 — Amine oxidase N-terminal region
Family Family family	d.17.2.1 — Amine oxidase N-terminal region

Domain ID domain_id	d1qaka4
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.82 — N domain of copper amine oxidase-like
Superfamily Superfamily superfamily	d.82.1 — Copper amine oxidase, domain N
Family Family family	d.82.1.1 — Copper amine oxidase, domain N

Domain ID domain_id	d1qakb1
Class class	b — All beta proteins
Fold Fold fold	b.30 — Supersandwich
Superfamily Superfamily superfamily	b.30.2 — Amine oxidase catalytic domain
Family Family family	b.30.2.1 — Amine oxidase catalytic domain

Domain ID domain_id	d1qakb2
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.17 — Cystatin-like
Superfamily Superfamily superfamily	d.17.2 — Amine oxidase N-terminal region
Family Family family	d.17.2.1 — Amine oxidase N-terminal region

Domain ID domain_id	d1qakb3
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.17 — Cystatin-like
Superfamily Superfamily superfamily	d.17.2 — Amine oxidase N-terminal region
Family Family family	d.17.2.1 — Amine oxidase N-terminal region

Domain ID domain_id	d1qakb4
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.82 — N domain of copper amine oxidase-like
Superfamily Superfamily superfamily	d.82.1 — Copper amine oxidase, domain N
Family Family family	d.82.1.1 — Copper amine oxidase, domain N

CATH v4.4 (8 domains)

Domain ID domain_id	1qakA01
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	457 — Copper Amine Oxidase; Chain A, domain 1
Homologous superfamily homologous superfamily	10 — Copper amine oxidase-like, N-terminal domain

Domain ID domain_id	1qakA02
Class class	3 — Alpha Beta
Architecture architecture	10 — Roll
Topology topology	450 — Nuclear Transport Factor 2; Chain: A,
Homologous superfamily homologous superfamily	40 —

Domain ID domain_id	1qakA03
Class class	2 — Mainly Beta
Architecture architecture	70 — Distorted Sandwich
Topology topology	98 — Beta-galactosidase; Chain A, domain 5
Homologous superfamily homologous superfamily	20 — Copper amine oxidase, catalytic domain

Domain ID domain_id	1qakA04
Class class	3 — Alpha Beta
Architecture architecture	10 — Roll
Topology topology	450 — Nuclear Transport Factor 2; Chain: A,
Homologous superfamily homologous superfamily	40 —

Domain ID domain_id	1qakB01
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	457 — Copper Amine Oxidase; Chain A, domain 1
Homologous superfamily homologous superfamily	10 — Copper amine oxidase-like, N-terminal domain

Domain ID domain_id	1qakB02
Class class	3 — Alpha Beta
Architecture architecture	10 — Roll
Topology topology	450 — Nuclear Transport Factor 2; Chain: A,
Homologous superfamily homologous superfamily	40 —

Domain ID domain_id	1qakB03
Class class	2 — Mainly Beta
Architecture architecture	70 — Distorted Sandwich
Topology topology	98 — Beta-galactosidase; Chain A, domain 5
Homologous superfamily homologous superfamily	20 — Copper amine oxidase, catalytic domain

Domain ID domain_id	1qakB04
Class class	3 — Alpha Beta
Architecture architecture	10 — Roll
Topology topology	450 — Nuclear Transport Factor 2; Chain: A,
Homologous superfamily homologous superfamily	40 —

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8. Citations (1)

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Unit-cell length a length_a	134.660 Å
Unit-cell length b length_b	166.170 Å
Unit-cell length c length_c	79.090 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	90.00 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	8

Space group space_group	P 21 21 21
Space-group number int_tables_number	19
Crystal system crystal_system	—

Resolution resolution	2.000 Å
Low-resolution limit resolution_low	20.000 Å
R factor r_factor	0.1790
R_work r_work	0.1764
R_free r_free	0.2443

fit	/app/data/saxs_computation/qa/1qak/1qak.fit
pddf	/app/data/pr_computation/qa/1qak/1qak.pr.out
profile	/app/data/saxs_computation/qa/1qak/1qak.dat