2wqt

Dodecahedral assembly of MhpD

Method: X-RAY DIFFRACTION

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

2-KETO-4-PENTENOATE HYDRATASE

ESCHERICHIA COLI

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein homooligomer	Homooligomer	Protein 60	PHOSPHATE ION × 114 SODIUM ION × 60 POTASSIUM ION × 60 water × 60	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	MHPD_ECOLI
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 2–270； UniProt 1–269 Author chain B； PDBConstruct 2–270； UniProt 1–269 Author chain C； PDBConstruct 2–270； UniProt 1–269 Author chain D； PDBConstruct 2–270； UniProt 1–269 Author chain E； PDBConstruct 2–270； UniProt 1–269 Author chain F； PDBConstruct 2–270； UniProt 1–269 Author chain G； PDBConstruct 2–270； UniProt 1–269 Author chain H； PDBConstruct 2–270； UniProt 1–269 Author chain I； PDBConstruct 2–270； UniProt 1–269 Author chain J； PDBConstruct 2–270； UniProt 1–269 Author chain K； PDBConstruct 2–270； UniProt 1–269 Author chain L； PDBConstruct 2–270； UniProt 1–269 Author chain M； PDBConstruct 2–270； UniProt 1–269 Author chain N； PDBConstruct 2–270； UniProt 1–269 Author chain O； PDBConstruct 2–270； UniProt 1–269 Author chain P； PDBConstruct 2–270； UniProt 1–269 Author chain Q； PDBConstruct 2–270； UniProt 1–269 Author chain R； PDBConstruct 2–270； UniProt 1–269 Author chain S； PDBConstruct 2–270； UniProt 1–269 Author chain T； PDBConstruct 2–270； UniProt 1–269

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	2wqt
Deposition date deposition_date	2009-08-27
Structure title title	Dodecahedral assembly of MhpD
Keywords keywords	LYASE, HYDRATASE, DODECAHEDRAL FORM, AROMATIC HYDROCARBONS CATABOLISM; LYASE
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.

2wqt__assembly_1__model_1

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

Download this curve (.dat)

2wqt__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

2wqt__assembly_1__model_1 | P(r) · Pending

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

Rg（Guinier）	90.73 Å
Rg (electron density)	89.17 Å
Total Rg	89.28 Å
Atom count	119838
Residues	15720
Excluded volume	2123100 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`2wqt__assembly_1__model_1`	60-meric （60）	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 (5)

Entity 1 Entity 1 polymer

Description description	2-KETO-4-PENTENOATE HYDRATASE
Molecular weight formula_weight	29033.0 kDa
EC 编号 ec_number	4.2.1.80
Source method src_method	man
Copy count entity_count	20

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B,C,D,E,F,G,H,I,J,K,L,M,N,O,P,Q,R,S,T
Atom count atom_count	40183

LMTKHTLEQLAADLRRAAEQGEAIAPLRDLIGIDNAEAAYAIQHINVQHDVAQGRRVVGRKVGLTHPKVQQQLGVDQPDFGTLFADMCYGDNEIIPFSRVLQPRIEAEIALVLNRDLPATDITFDELYNAIEWVLPALEVVGSRIRDWSIQFVDTVADNASCGVYVIGGPAQRPAGLDLKNCAMKMTRNNEEVSSGRGSECLGHPLNAAVWLARKMASLGEPLRTGDIILTGALGPMVAVNAGDRFEAHIEGIGSVAATFSSAAPKGSLS

Source Source

Source organism organism	ESCHERICHIA COLI
NCBI taxonomy ID ncbi_taxonomy_id	83333
Host organism host_organism	ESCHERICHIA COLI

Entity 2 Entity 2 non-polymer

Description description	PHOSPHATE ION
Molecular weight formula_weight	95.0 kDa
Source method src_method	syn
Copy count entity_count	38

Entity 3 Entity 3 non-polymer

Description description	SODIUM ION
Molecular weight formula_weight	23.0 kDa
Source method src_method	syn
Copy count entity_count	20

Entity 4 Entity 4 non-polymer

Description description	POTASSIUM ION
Molecular weight formula_weight	39.1 kDa
Source method src_method	syn
Copy count entity_count	20

Entity 5 Entity 5 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	233

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6. Fold Classification (SCOP + CATH) 40 domains

SCOP 2.08 (20 domains)

Domain ID domain_id	d2wqta_
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.177 — FAH
Superfamily Superfamily superfamily	d.177.1 — FAH
Family Family family	d.177.1.1 — FAH

Domain ID domain_id	d2wqtb_
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.177 — FAH
Superfamily Superfamily superfamily	d.177.1 — FAH
Family Family family	d.177.1.1 — FAH

Domain ID domain_id	d2wqtc_
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.177 — FAH
Superfamily Superfamily superfamily	d.177.1 — FAH
Family Family family	d.177.1.1 — FAH

Domain ID domain_id	d2wqtd_
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.177 — FAH
Superfamily Superfamily superfamily	d.177.1 — FAH
Family Family family	d.177.1.1 — FAH

Domain ID domain_id	d2wqte_
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.177 — FAH
Superfamily Superfamily superfamily	d.177.1 — FAH
Family Family family	d.177.1.1 — FAH

Domain ID domain_id	d2wqtf_
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.177 — FAH
Superfamily Superfamily superfamily	d.177.1 — FAH
Family Family family	d.177.1.1 — FAH

Domain ID domain_id	d2wqtg_
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.177 — FAH
Superfamily Superfamily superfamily	d.177.1 — FAH
Family Family family	d.177.1.1 — FAH

Domain ID domain_id	d2wqth_
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.177 — FAH
Superfamily Superfamily superfamily	d.177.1 — FAH
Family Family family	d.177.1.1 — FAH

Domain ID domain_id	d2wqti_
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.177 — FAH
Superfamily Superfamily superfamily	d.177.1 — FAH
Family Family family	d.177.1.1 — FAH

Domain ID domain_id	d2wqtj_
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.177 — FAH
Superfamily Superfamily superfamily	d.177.1 — FAH
Family Family family	d.177.1.1 — FAH

Domain ID domain_id	d2wqtk_
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.177 — FAH
Superfamily Superfamily superfamily	d.177.1 — FAH
Family Family family	d.177.1.1 — FAH

Domain ID domain_id	d2wqtl_
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.177 — FAH
Superfamily Superfamily superfamily	d.177.1 — FAH
Family Family family	d.177.1.1 — FAH

Domain ID domain_id	d2wqtm_
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.177 — FAH
Superfamily Superfamily superfamily	d.177.1 — FAH
Family Family family	d.177.1.1 — FAH

Domain ID domain_id	d2wqtn_
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.177 — FAH
Superfamily Superfamily superfamily	d.177.1 — FAH
Family Family family	d.177.1.1 — FAH

Domain ID domain_id	d2wqto_
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.177 — FAH
Superfamily Superfamily superfamily	d.177.1 — FAH
Family Family family	d.177.1.1 — FAH

Domain ID domain_id	d2wqtp_
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.177 — FAH
Superfamily Superfamily superfamily	d.177.1 — FAH
Family Family family	d.177.1.1 — FAH

Domain ID domain_id	d2wqtq_
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.177 — FAH
Superfamily Superfamily superfamily	d.177.1 — FAH
Family Family family	d.177.1.1 — FAH

Domain ID domain_id	d2wqtr_
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.177 — FAH
Superfamily Superfamily superfamily	d.177.1 — FAH
Family Family family	d.177.1.1 — FAH

Domain ID domain_id	d2wqts_
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.177 — FAH
Superfamily Superfamily superfamily	d.177.1 — FAH
Family Family family	d.177.1.1 — FAH

Domain ID domain_id	d2wqtt_
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.177 — FAH
Superfamily Superfamily superfamily	d.177.1 — FAH
Family Family family	d.177.1.1 — FAH

CATH v4.4 (20 domains)

Domain ID domain_id	2wqtA00
Class class	3 — Alpha Beta
Architecture architecture	90 — Alpha-Beta Complex
Topology topology	850 — Fumarylacetoacetate hydrolase; domain 2
Homologous superfamily homologous superfamily	10 — Fumarylacetoacetase-like, C-terminal domain

Domain ID domain_id	2wqtB00
Class class	3 — Alpha Beta
Architecture architecture	90 — Alpha-Beta Complex
Topology topology	850 — Fumarylacetoacetate hydrolase; domain 2
Homologous superfamily homologous superfamily	10 — Fumarylacetoacetase-like, C-terminal domain

Domain ID domain_id	2wqtC00
Class class	3 — Alpha Beta
Architecture architecture	90 — Alpha-Beta Complex
Topology topology	850 — Fumarylacetoacetate hydrolase; domain 2
Homologous superfamily homologous superfamily	10 — Fumarylacetoacetase-like, C-terminal domain

Domain ID domain_id	2wqtD00
Class class	3 — Alpha Beta
Architecture architecture	90 — Alpha-Beta Complex
Topology topology	850 — Fumarylacetoacetate hydrolase; domain 2
Homologous superfamily homologous superfamily	10 — Fumarylacetoacetase-like, C-terminal domain

Domain ID domain_id	2wqtE00
Class class	3 — Alpha Beta
Architecture architecture	90 — Alpha-Beta Complex
Topology topology	850 — Fumarylacetoacetate hydrolase; domain 2
Homologous superfamily homologous superfamily	10 — Fumarylacetoacetase-like, C-terminal domain

Domain ID domain_id	2wqtF00
Class class	3 — Alpha Beta
Architecture architecture	90 — Alpha-Beta Complex
Topology topology	850 — Fumarylacetoacetate hydrolase; domain 2
Homologous superfamily homologous superfamily	10 — Fumarylacetoacetase-like, C-terminal domain

Domain ID domain_id	2wqtG00
Class class	3 — Alpha Beta
Architecture architecture	90 — Alpha-Beta Complex
Topology topology	850 — Fumarylacetoacetate hydrolase; domain 2
Homologous superfamily homologous superfamily	10 — Fumarylacetoacetase-like, C-terminal domain

Domain ID domain_id	2wqtH00
Class class	3 — Alpha Beta
Architecture architecture	90 — Alpha-Beta Complex
Topology topology	850 — Fumarylacetoacetate hydrolase; domain 2
Homologous superfamily homologous superfamily	10 — Fumarylacetoacetase-like, C-terminal domain

Domain ID domain_id	2wqtI00
Class class	3 — Alpha Beta
Architecture architecture	90 — Alpha-Beta Complex
Topology topology	850 — Fumarylacetoacetate hydrolase; domain 2
Homologous superfamily homologous superfamily	10 — Fumarylacetoacetase-like, C-terminal domain

Domain ID domain_id	2wqtJ00
Class class	3 — Alpha Beta
Architecture architecture	90 — Alpha-Beta Complex
Topology topology	850 — Fumarylacetoacetate hydrolase; domain 2
Homologous superfamily homologous superfamily	10 — Fumarylacetoacetase-like, C-terminal domain

Domain ID domain_id	2wqtK00
Class class	3 — Alpha Beta
Architecture architecture	90 — Alpha-Beta Complex
Topology topology	850 — Fumarylacetoacetate hydrolase; domain 2
Homologous superfamily homologous superfamily	10 — Fumarylacetoacetase-like, C-terminal domain

Domain ID domain_id	2wqtL00
Class class	3 — Alpha Beta
Architecture architecture	90 — Alpha-Beta Complex
Topology topology	850 — Fumarylacetoacetate hydrolase; domain 2
Homologous superfamily homologous superfamily	10 — Fumarylacetoacetase-like, C-terminal domain

Domain ID domain_id	2wqtM00
Class class	3 — Alpha Beta
Architecture architecture	90 — Alpha-Beta Complex
Topology topology	850 — Fumarylacetoacetate hydrolase; domain 2
Homologous superfamily homologous superfamily	10 — Fumarylacetoacetase-like, C-terminal domain

Domain ID domain_id	2wqtN00
Class class	3 — Alpha Beta
Architecture architecture	90 — Alpha-Beta Complex
Topology topology	850 — Fumarylacetoacetate hydrolase; domain 2
Homologous superfamily homologous superfamily	10 — Fumarylacetoacetase-like, C-terminal domain

Domain ID domain_id	2wqtO00
Class class	3 — Alpha Beta
Architecture architecture	90 — Alpha-Beta Complex
Topology topology	850 — Fumarylacetoacetate hydrolase; domain 2
Homologous superfamily homologous superfamily	10 — Fumarylacetoacetase-like, C-terminal domain

Domain ID domain_id	2wqtP00
Class class	3 — Alpha Beta
Architecture architecture	90 — Alpha-Beta Complex
Topology topology	850 — Fumarylacetoacetate hydrolase; domain 2
Homologous superfamily homologous superfamily	10 — Fumarylacetoacetase-like, C-terminal domain

Domain ID domain_id	2wqtQ00
Class class	3 — Alpha Beta
Architecture architecture	90 — Alpha-Beta Complex
Topology topology	850 — Fumarylacetoacetate hydrolase; domain 2
Homologous superfamily homologous superfamily	10 — Fumarylacetoacetase-like, C-terminal domain

Domain ID domain_id	2wqtR00
Class class	3 — Alpha Beta
Architecture architecture	90 — Alpha-Beta Complex
Topology topology	850 — Fumarylacetoacetate hydrolase; domain 2
Homologous superfamily homologous superfamily	10 — Fumarylacetoacetase-like, C-terminal domain

Domain ID domain_id	2wqtS00
Class class	3 — Alpha Beta
Architecture architecture	90 — Alpha-Beta Complex
Topology topology	850 — Fumarylacetoacetate hydrolase; domain 2
Homologous superfamily homologous superfamily	10 — Fumarylacetoacetase-like, C-terminal domain

Domain ID domain_id	2wqtT00
Class class	3 — Alpha Beta
Architecture architecture	90 — Alpha-Beta Complex
Topology topology	850 — Fumarylacetoacetate hydrolase; domain 2
Homologous superfamily homologous superfamily	10 — Fumarylacetoacetase-like, C-terminal domain

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Unit-cell length a length_a	207.350 Å
Unit-cell length b length_b	207.350 Å
Unit-cell length c length_c	545.471 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	90.00 °
Unit-cell angle γ angle_gamma	120.00 °
Molecules per unit cell Z z_pdb	180

Space group space_group	H 3
Space-group number int_tables_number	146
Crystal system crystal_system	—

Resolution resolution	2.800 Å
Low-resolution limit resolution_low	35.260 Å
R factor r_factor	0.2225
R_work r_work	0.2219
R_free r_free	0.2338

Dodecahedral assembly of MhpD

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

2-KETO-4-PENTENOATE HYDRATASE

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

2wqt__assembly_1__model_1

2wqt__assembly_1__model_1 | I(q)

2wqt__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 (5)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 non-polymer

Entity 3 Entity 3 non-polymer

Entity 4 Entity 4 non-polymer

Entity 5 Entity 5 water

6. Fold Classification (SCOP + CATH) 40 domains

SCOP 2.08 (20 domains)

CATH v4.4 (20 domains)

7. Citations (1)

Dodecahedral assembly of MhpD

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

2-KETO-4-PENTENOATE HYDRATASE

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

2wqt__assembly_1__model_1

2wqt__assembly_1__model_1 | I(q)

2wqt__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 (5)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 non-polymer

Entity 3 Entity 3 non-polymer

Entity 4 Entity 4 non-polymer

Entity 5 Entity 5 water

6. Fold Classification (SCOP + CATH) 40 domains

SCOP 2.08 (20 domains)

CATH v4.4 (20 domains)

7. Citations (1)