1t3q

Crystal structure of quinoline 2-Oxidoreductase from Pseudomonas Putida 86

Method: X-RAY DIFFRACTION

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

quinoline 2-oxidoreductase small subunit

OrganismNot specified

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 6	quinoline 2-oxidoreductase large subunit × 2 （P72224） quinoline 2-oxidoreductase medium subunit × 2 （P72222） FE2/S2 (INORGANIC) CLUSTER × 4 GLYCEROL × 9 SULFATE ION × 8 PTERIN CYTOSINE DINUCLEOTIDE × 2 DIOXOSULFIDOMOLYBDENUM(VI) ION × 2 FLAVIN-ADENINE DINUCLEOTIDE × 2 water × 6	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	P72223_PSEPU
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–168； UniProt 1–168 Author chain D； PDBConstruct 1–168； UniProt 1–168

quinoline 2-oxidoreductase large subunit

OrganismNot specified

UniProt P72224

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 6	quinoline 2-oxidoreductase small subunit × 2 （P72223） quinoline 2-oxidoreductase medium subunit × 2 （P72222） FE2/S2 (INORGANIC) CLUSTER × 4 GLYCEROL × 9 SULFATE ION × 8 PTERIN CYTOSINE DINUCLEOTIDE × 2 DIOXOSULFIDOMOLYBDENUM(VI) ION × 2 FLAVIN-ADENINE DINUCLEOTIDE × 2 water × 6	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	P72224_PSEPU
Isoform	—
PDB entities	2
Chains and sequence ranges	Author chain B； PDBConstruct 1–788； UniProt 1–788 Author chain E； PDBConstruct 1–788； UniProt 1–788

quinoline 2-oxidoreductase medium subunit

OrganismNot specified

UniProt P72222

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 6	quinoline 2-oxidoreductase small subunit × 2 （P72223） quinoline 2-oxidoreductase large subunit × 2 （P72224） FE2/S2 (INORGANIC) CLUSTER × 4 GLYCEROL × 9 SULFATE ION × 8 PTERIN CYTOSINE DINUCLEOTIDE × 2 DIOXOSULFIDOMOLYBDENUM(VI) ION × 2 FLAVIN-ADENINE DINUCLEOTIDE × 2 water × 6	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	P72222_PSEPU
Isoform	—
PDB entities	3
Chains and sequence ranges	Author chain C； PDBConstruct 1–288； UniProt 1–288 Author chain F； PDBConstruct 1–288； UniProt 1–288

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.

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2. Structure Basics 2. Structure Basics

Entry ID entry_id	1t3q
Deposition date deposition_date	2004-04-27
Structure title title	Crystal structure of quinoline 2-Oxidoreductase from Pseudomonas Putida 86
Keywords keywords	QOR, MOLYBDENUM, MCD, OXIDOREDUCTASE; OXIDOREDUCTASE
Experimental Method method	X-RAY DIFFRACTION

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3. Official assembly/model SAXS Official SAXS Profiles

This page reads only the latest assembly calculations. Every curve maps to an explicit PDB entry, official biological assembly and coordinate model.

1t3q__assembly_1__model_1

Assembly 1 · Model 1 · CRYSOL 4.1.3-1-20251215 (887e7ef)

Download this curve (.dat)

1t3q__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

1t3q__assembly_1__model_1 | P(r) · Pending

P(r) will be calculated and displayed separately for the same assembly/model.

Rg（Guinier）	43.60 Å
Rg (electron density)	43.57 Å
Total Rg	43.62 Å
Atom count	18790
Residues	2466
Excluded volume	333610 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`1t3q__assembly_1__model_1`	hexameric （6）	Success	4.1.3-1-20251215 (887e7ef)	View Download

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4. Crystallography and Experiment 4. Crystallography & Experiment

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5. Entities and Polymers Entities & Polymers (10)

Entity 1 Entity 1 polymer

Description description	quinoline 2-oxidoreductase small subunit
Molecular weight formula_weight	18043.6 kDa
EC 编号 ec_number	1.3.99.17
Source method src_method	nat
Copy count entity_count	2

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,D
Atom count atom_count	21323

MQAHEESQLMRISATINGKPRVFYVEPRMHLADALREVVGLTGTKIGCEQGVCGSCTILIDGAPMRSCLTLAVQAEGCSIETVEGLSQGEKLNALQDSFRRHHALQCGFCTAGMLATARSILAENPAPSRDEVREVMSGNLCRCTGYETIIDAITDPAVAEAARRGEV

Entity 2 Entity 2 polymer

Description description	quinoline 2-oxidoreductase large subunit
Molecular weight formula_weight	84257.8 kDa
EC 编号 ec_number	1.3.99.17
Source method src_method	nat
Copy count entity_count	2

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	B,E

MMKHEVVALKKKSIGTSVLRREDTRLLTGRGRYIADLVLSGMLHVASLRSPFAHARIVSIDVADAQALPGVELVWCGADVAELSQGIVATMQVEGFQTTIQPLLANGVTRFVGEIVAVVVASSRAIAEDAAQLIQVEYEELPAVTGIEAALEGEARANDTLAGNVVSRTSRARDELAPIFASSAGVVRGQFSCGRVSACPMETRGAVAQYEWTTQQLILWTATQMPSFVRTMVAMFCAIPEHLIEVRVPDVGGGFGQKAHLHPEELLVCLLSRALGRPVRWIEDRQENFLGATHAKQQRNEMGLAFDGDGRFLALENRSITDGGAYNNLPWTQLVESHVGNAVILGVYKVPAVSEESIAVATNKCPIGAYRGVGFTAGQIARETLIDRAARQLGLSPFEIRRRNVVMPEDFPFTNRLGQTHREGTYLQTINLLEEMVNPEAFRQRQAEARARGKYLGLGVSVFNEVTGTGTRTLSFLGTPTTTHDSATVRIDPTGKVTVTTSLASSGQGHETTLAQIAADVLGVPASDVVIQAGSTKNTYGFGAYASRGAVIGAGSIGRAASIVRERVKQLAGHLLEAASEDIVIEDGLVHVAGVPAKGMPFAEVVGAAYFADATHPPGFDATLEATATYDPSDLVLANGGHAAIVEIDASTYATRVTDFFAVEDCGTMINPMIVEGQIRGGIAQAIGQTLLEEVIYDDFGQLVTTTLMDYLIPTTLDVPDIRIRHLETPSPLVPGGIKGMGESAMISAPAAVVAAVNDALAHLEVVIETVPITPERIFRSIQERPMQ

Entity 3 Entity 3 polymer

Description description	quinoline 2-oxidoreductase medium subunit
Molecular weight formula_weight	30705.4 kDa
EC 编号 ec_number	1.3.99.17
Source method src_method	nat
Copy count entity_count	2

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	C,F

MKFPAFSYRAPASLQEVIQVLADDPDARIIAGGQSLLPLLAFRLVYPSCLVDLRNVSELFEISQSAGILSVGAMVTHFRNKTDPTVAKCVPILPKVLAHVAHQAVRNRGTLGGSLAHADAGAEMPFLMATLGATMYIASSAGVRSVSATDFMKGHYFTDLEAGEVLVRVEIPIPALHWEFDEYARRKGDYALVMAAAGLSMQGGRCVAARIALGAVEERAHQAIRANDFLVGKVIDESTAATAAELATEGLEPRSDIHGSRDLRLSLAKAITQRVILKAAQGAMYAGA

Entity 4 Entity 4 non-polymer

Description description	FE2/S2 (INORGANIC) CLUSTER
Molecular weight formula_weight	175.8 kDa
Source method src_method	syn
Copy count entity_count	4

Entity 5 Entity 5 non-polymer

Description description	GLYCEROL
Molecular weight formula_weight	92.1 kDa
Source method src_method	syn
Copy count entity_count	9

Entity 6 Entity 6 non-polymer

Description description	SULFATE ION
Molecular weight formula_weight	96.1 kDa
Source method src_method	syn
Copy count entity_count	8

Entity 7 Entity 7 non-polymer

Description description	PTERIN CYTOSINE DINUCLEOTIDE
Molecular weight formula_weight	696.5 kDa
Source method src_method	syn
Copy count entity_count	2

Entity 8 Entity 8 non-polymer

Description description	DIOXOSULFIDOMOLYBDENUM(VI) ION
Molecular weight formula_weight	160.0 kDa
Source method src_method	syn
Copy count entity_count	2

Entity 9 Entity 9 non-polymer

Description description	FLAVIN-ADENINE DINUCLEOTIDE
Molecular weight formula_weight	785.5 kDa
Source method src_method	syn
Copy count entity_count	2

Entity 10 Entity 10 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	2533

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6. Fold Classification (SCOP + CATH) 28 domains

SCOP 2.08 (12 domains)

Domain ID domain_id	d1t3qa1
Class class	a — All alpha proteins
Fold Fold fold	a.56 — CO dehydrogenase ISP C-domain like
Superfamily Superfamily superfamily	a.56.1 — CO dehydrogenase ISP C-domain like
Family Family family	a.56.1.1 — CO dehydrogenase ISP C-domain like

Domain ID domain_id	d1t3qa2
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.15 — beta-Grasp (ubiquitin-like)
Superfamily Superfamily superfamily	d.15.4 — 2Fe-2S ferredoxin-like
Family Family family	d.15.4.2 — 2Fe-2S ferredoxin domains from multidomain proteins

Domain ID domain_id	d1t3qb1
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.41 — alpha/beta-Hammerhead
Superfamily Superfamily superfamily	d.41.1 — CO dehydrogenase molybdoprotein N-domain-like
Family Family family	d.41.1.1 — CO dehydrogenase molybdoprotein N-domain-like

Domain ID domain_id	d1t3qb2
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.133 — Molybdenum cofactor-binding domain
Superfamily Superfamily superfamily	d.133.1 — Molybdenum cofactor-binding domain
Family Family family	d.133.1.1 — Molybdenum cofactor-binding domain

Domain ID domain_id	d1t3qc1
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.87 — CO dehydrogenase flavoprotein C-domain-like
Superfamily Superfamily superfamily	d.87.2 — CO dehydrogenase flavoprotein C-terminal domain-like
Family Family family	d.87.2.1 — CO dehydrogenase flavoprotein C-terminal domain-like

Domain ID domain_id	d1t3qc2
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.145 — FAD-binding/transporter-associated domain-like
Superfamily Superfamily superfamily	d.145.1 — FAD-binding/transporter-associated domain-like
Family Family family	d.145.1.3 — CO dehydrogenase flavoprotein N-terminal domain-like

Domain ID domain_id	d1t3qd1
Class class	a — All alpha proteins
Fold Fold fold	a.56 — CO dehydrogenase ISP C-domain like
Superfamily Superfamily superfamily	a.56.1 — CO dehydrogenase ISP C-domain like
Family Family family	a.56.1.1 — CO dehydrogenase ISP C-domain like

Domain ID domain_id	d1t3qd2
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.15 — beta-Grasp (ubiquitin-like)
Superfamily Superfamily superfamily	d.15.4 — 2Fe-2S ferredoxin-like
Family Family family	d.15.4.2 — 2Fe-2S ferredoxin domains from multidomain proteins

Domain ID domain_id	d1t3qe1
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.41 — alpha/beta-Hammerhead
Superfamily Superfamily superfamily	d.41.1 — CO dehydrogenase molybdoprotein N-domain-like
Family Family family	d.41.1.1 — CO dehydrogenase molybdoprotein N-domain-like

Domain ID domain_id	d1t3qe2
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.133 — Molybdenum cofactor-binding domain
Superfamily Superfamily superfamily	d.133.1 — Molybdenum cofactor-binding domain
Family Family family	d.133.1.1 — Molybdenum cofactor-binding domain

Domain ID domain_id	d1t3qf1
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.87 — CO dehydrogenase flavoprotein C-domain-like
Superfamily Superfamily superfamily	d.87.2 — CO dehydrogenase flavoprotein C-terminal domain-like
Family Family family	d.87.2.1 — CO dehydrogenase flavoprotein C-terminal domain-like

Domain ID domain_id	d1t3qf2
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.145 — FAD-binding/transporter-associated domain-like
Superfamily Superfamily superfamily	d.145.1 — FAD-binding/transporter-associated domain-like
Family Family family	d.145.1.3 — CO dehydrogenase flavoprotein N-terminal domain-like

CATH v4.4 (16 domains)

Domain ID domain_id	1t3qA01
Class class	3 — Alpha Beta
Architecture architecture	10 — Roll
Topology topology	20 — Ubiquitin-like (UB roll)
Homologous superfamily homologous superfamily	30 — Beta-grasp domain

Domain ID domain_id	1t3qA02
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	150 — DNA polymerase; domain 1
Homologous superfamily homologous superfamily	120 — [2Fe-2S]-binding domain

Domain ID domain_id	1t3qB01
Class class	3 — Alpha Beta
Architecture architecture	90 — Alpha-Beta Complex
Topology topology	1170 — Aldehyde Oxidoreductase; domain 3
Homologous superfamily homologous superfamily	50 — Aldehyde oxidase/xanthine dehydrogenase, a/b hammerhead

Domain ID domain_id	1t3qB03
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	365 — Aldehyde Oxidoreductase; domain 4
Homologous superfamily homologous superfamily	10 — Aldehyde oxidase/xanthine dehydrogenase, molybdopterin binding domain

Domain ID domain_id	1t3qB04
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	365 — Aldehyde Oxidoreductase; domain 4
Homologous superfamily homologous superfamily	10 — Aldehyde oxidase/xanthine dehydrogenase, molybdopterin binding domain

Domain ID domain_id	1t3qC01
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	43 — Uridine Diphospho-n-acetylenolpyruvylglucosamine Reductase; domain 2
Homologous superfamily homologous superfamily	10 — Uridine Diphospho-n-acetylenolpyruvylglucosamine Reductase, domain 2

Domain ID domain_id	1t3qC02
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	465 — Uridine Diphospho-n-acetylenolpyruvylglucosamine Reductase; domain 3
Homologous superfamily homologous superfamily	10 —

Domain ID domain_id	1t3qC03
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	390 — Enolase-like; domain 1
Homologous superfamily homologous superfamily	50 — CO dehydrogenase flavoprotein, C-terminal domain

Domain ID domain_id	1t3qD01
Class class	3 — Alpha Beta
Architecture architecture	10 — Roll
Topology topology	20 — Ubiquitin-like (UB roll)
Homologous superfamily homologous superfamily	30 — Beta-grasp domain

Domain ID domain_id	1t3qD02
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	150 — DNA polymerase; domain 1
Homologous superfamily homologous superfamily	120 — [2Fe-2S]-binding domain

Domain ID domain_id	1t3qE01
Class class	3 — Alpha Beta
Architecture architecture	90 — Alpha-Beta Complex
Topology topology	1170 — Aldehyde Oxidoreductase; domain 3
Homologous superfamily homologous superfamily	50 — Aldehyde oxidase/xanthine dehydrogenase, a/b hammerhead

Domain ID domain_id	1t3qE03
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	365 — Aldehyde Oxidoreductase; domain 4
Homologous superfamily homologous superfamily	10 — Aldehyde oxidase/xanthine dehydrogenase, molybdopterin binding domain

Domain ID domain_id	1t3qE04
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	365 — Aldehyde Oxidoreductase; domain 4
Homologous superfamily homologous superfamily	10 — Aldehyde oxidase/xanthine dehydrogenase, molybdopterin binding domain

Domain ID domain_id	1t3qF01
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	43 — Uridine Diphospho-n-acetylenolpyruvylglucosamine Reductase; domain 2
Homologous superfamily homologous superfamily	10 — Uridine Diphospho-n-acetylenolpyruvylglucosamine Reductase, domain 2

Domain ID domain_id	1t3qF02
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	465 — Uridine Diphospho-n-acetylenolpyruvylglucosamine Reductase; domain 3
Homologous superfamily homologous superfamily	10 —

Domain ID domain_id	1t3qF03
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	390 — Enolase-like; domain 1
Homologous superfamily homologous superfamily	50 — CO dehydrogenase flavoprotein, C-terminal domain

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Unit-cell length a length_a	278.320 Å
Unit-cell length b length_b	72.100 Å
Unit-cell length c length_c	202.650 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	127.98 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	8

Space group space_group	C 1 2 1
Space-group number int_tables_number	5
Crystal system crystal_system	—

Resolution resolution	1.800 Å
Low-resolution limit resolution_low	19.290 Å
R factor r_factor	0.1860
R_work r_work	0.1860
R_free r_free	0.2070

Crystal structure of quinoline 2-Oxidoreductase from Pseudomonas Putida 86

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

quinoline 2-oxidoreductase small subunit

State in the Current Structure

Other States of the Same Protein in the Database

quinoline 2-oxidoreductase large subunit

State in the Current Structure

Other States of the Same Protein in the Database

quinoline 2-oxidoreductase medium subunit

State in the Current Structure

Other States of the Same Protein in the Database

2. Structure Basics 2. Structure Basics

3. Official assembly/model SAXS Official SAXS Profiles

1t3q__assembly_1__model_1

1t3q__assembly_1__model_1 | I(q)

1t3q__assembly_1__model_1 | P(r) · Pending

4. Crystallography and Experiment 4. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

Refinement Refinement

Diffraction experiment Diffraction

5. Entities and Polymers Entities & Polymers (10)

Entity 1 Entity 1 polymer

Polymer Polymer

Entity 2 Entity 2 polymer

Polymer Polymer

Entity 3 Entity 3 polymer

Polymer Polymer

Entity 4 Entity 4 non-polymer

Entity 5 Entity 5 non-polymer

Entity 6 Entity 6 non-polymer

Entity 7 Entity 7 non-polymer

Entity 8 Entity 8 non-polymer

Entity 9 Entity 9 non-polymer

Entity 10 Entity 10 water

6. Fold Classification (SCOP + CATH) 28 domains

SCOP 2.08 (12 domains)

CATH v4.4 (16 domains)

7. Citations (1)

Crystal structure of quinoline 2-Oxidoreductase from Pseudomonas Putida 86

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

quinoline 2-oxidoreductase small subunit

State in the Current Structure

Other States of the Same Protein in the Database

Monomer

Homodimer

Homotetramer

Other homooligomers

Heteromeric or nucleic-acid complex

quinoline 2-oxidoreductase large subunit

State in the Current Structure

Other States of the Same Protein in the Database

Monomer

Homodimer

Homotetramer

Other homooligomers

Heteromeric or nucleic-acid complex

quinoline 2-oxidoreductase medium subunit

State in the Current Structure

Other States of the Same Protein in the Database

Monomer

Homodimer

Homotetramer

Other homooligomers

Heteromeric or nucleic-acid complex

2. Structure Basics 2. Structure Basics

3. Official assembly/model SAXS Official SAXS Profiles

1t3q__assembly_1__model_1

1t3q__assembly_1__model_1 | I(q)

1t3q__assembly_1__model_1 | P(r) · Pending

4. Crystallography and Experiment 4. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

Refinement Refinement

Diffraction experiment Diffraction

5. Entities and Polymers Entities & Polymers (10)

Entity 1 Entity 1 polymer

Polymer Polymer

Entity 2 Entity 2 polymer

Polymer Polymer

Entity 3 Entity 3 polymer

Polymer Polymer

Entity 4 Entity 4 non-polymer

Entity 5 Entity 5 non-polymer

Entity 6 Entity 6 non-polymer

Entity 7 Entity 7 non-polymer

Entity 8 Entity 8 non-polymer

Entity 9 Entity 9 non-polymer

Entity 10 Entity 10 water

6. Fold Classification (SCOP + CATH) 28 domains

SCOP 2.08 (12 domains)

CATH v4.4 (16 domains)

7. Citations (1)