1gtt

CRYSTAL STRUCTURE OF HPCE

Method: X-RAY DIFFRACTION

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

4-HYDROXYPHENYLACETATE DEGRADATION BIFUNCTIONAL ISOMERASE/DECARBOXYLASE

ESCHERICHIA COLI

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein monomer	Monomer	Protein 1	CALCIUM ION × 1 water × 1	Consistent with protein count
2	Protein monomer	Monomer	Protein 1	CALCIUM ION × 1 water × 1	Consistent with protein count
3	Protein monomer	Monomer	Protein 1	CALCIUM ION × 1 water × 1	Consistent with protein count
4	Protein monomer	Monomer	Protein 1	CALCIUM ION × 1 water × 1	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	HPAG_ECOLI
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–429； UniProt 1–429 Author chain B； PDBConstruct 1–429； UniProt 1–429 Author chain C； PDBConstruct 1–429； UniProt 1–429 Author chain D； PDBConstruct 1–429； UniProt 1–429

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	1gtt
Deposition date deposition_date	2002-01-18
Structure title title	CRYSTAL STRUCTURE OF HPCE
Keywords keywords	ISOMERASE, LYASE, BIFUNCTIONAL ENZYME, MULTIFUNCTIONAL ENZYME DECARBOXYLASE, AROMATIC HYDROCARBONS CATABOLISM; ISOMERASE
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.

1gtt__assembly_1__model_1

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

Download this curve (.dat)

1gtt__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

1gtt__assembly_1__model_1 | P(r) · Pending

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

Rg（Guinier）	22.64 Å
Rg (electron density)	21.36 Å
Total Rg	22.18 Å
Atom count	3252
Residues	421
Excluded volume	57853 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`1gtt__assembly_1__model_1`	monomeric （1）	Success	4.1.3-1-20251215 (887e7ef)	View Download
2	1	`1gtt__assembly_2__model_1`	monomeric （1）	Success	4.1.3-1-20251215 (887e7ef)	View Download
3	1	`1gtt__assembly_3__model_1`	monomeric （1）	Success	4.1.3-1-20251215 (887e7ef)	View Download
4	1	`1gtt__assembly_4__model_1`	monomeric （1）	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 (3)

Entity 1 Entity 1 polymer

Description description	4-HYDROXYPHENYLACETATE DEGRADATION BIFUNCTIONAL ISOMERASE/DECARBOXYLASE
Molecular weight formula_weight	47154.2 kDa
EC 编号 ec_number	5.3.3.10, 4.1.1.-
Source method src_method	man
Copy count entity_count	4

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B,C,D
Atom count atom_count	14274

MKGTIFAVALNHRSQLDAWQEAFQQSPYKAPPKTAVWFIKPRNTVIGCGEPIPFPQGEKVLSGATVALIVGKTATKVREEDAAEYIAGYALANDVSLPEESFYRPAIKAKCRDGFCPIGETVALSNVDNLTIYTEINGRPADHWNTADLQRNAAQLLSALSEFATLNPGDAILLGTPQARVEIQPGDRVRVLAEGFPPLENPVVDEREVTTRKSFPTLPHPHGTLFALGLNYADHASELEFKPPEEPLVFLKAPNTLTGDNQTSVRPNNIEYMHYEAELVVVIGKQARNVSEADAMDYVAGYTVCNDYAIRDYLENYYRPNLRVKSRDGLTPMLSTIVPKEAIPDPHNLTLRTFVNGELRQQGTTADLIFSVPFLIAYLSEFMTLNPGDMIATGTPKGLSDVVPGDEVVVEVEGVGRLVNRIVSEETAK

Source Source

Source organism organism	ESCHERICHIA COLI
NCBI taxonomy ID ncbi_taxonomy_id	562
Host organism host_organism	ESCHERICHIA COLI

Entity 2 Entity 2 non-polymer

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

Entity 3 Entity 3 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	1217

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6. Fold Classification (SCOP + CATH) 16 domains

SCOP 2.08 (8 domains)

Domain ID domain_id	d1gtta1
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	d1gtta2
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	d1gttb1
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	d1gttb2
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	d1gttc1
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	d1gttc2
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	d1gttd1
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	d1gttd2
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 (8 domains)

Domain ID domain_id	1gttA01
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	1gttA02
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	1gttB01
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	1gttB02
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	1gttC01
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	1gttC02
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	1gttD01
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	1gttD02
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	126.084 Å
Unit-cell length b length_b	138.201 Å
Unit-cell length c length_c	103.973 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	16

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

Resolution resolution	1.700 Å
Low-resolution limit resolution_low	91.290 Å
R factor r_factor	0.2170
R_work r_work	0.2160
R_free r_free	0.2520

CRYSTAL STRUCTURE OF HPCE

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

4-HYDROXYPHENYLACETATE DEGRADATION BIFUNCTIONAL ISOMERASE/DECARBOXYLASE

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

1gtt__assembly_1__model_1

1gtt__assembly_1__model_1 | I(q)

1gtt__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 (3)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 non-polymer

Entity 3 Entity 3 water

6. Fold Classification (SCOP + CATH) 16 domains

SCOP 2.08 (8 domains)

CATH v4.4 (8 domains)

7. Citations (1)

CRYSTAL STRUCTURE OF HPCE

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

4-HYDROXYPHENYLACETATE DEGRADATION BIFUNCTIONAL ISOMERASE/DECARBOXYLASE

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

1gtt__assembly_1__model_1

1gtt__assembly_1__model_1 | I(q)

1gtt__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 (3)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 non-polymer

Entity 3 Entity 3 water

6. Fold Classification (SCOP + CATH) 16 domains

SCOP 2.08 (8 domains)

CATH v4.4 (8 domains)

7. Citations (1)