SAXSdb — 1iuo

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

meta-Cleavage product hydrolase

Pseudomonas fluorescens

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein homooligomer	Homooligomer	Protein 2	ACETATE ION × 4 water × 2	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	P96965_PSEFL
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–282； UniProt 1–282

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	1iuo
Deposition date deposition_date	2002-03-06
Structure title title	meta-Cleavage product hydrolase from Pseudomonas fluorescens IP01 (CumD) S103A mutant complexed with acetates
Keywords keywords	;aromatic compounds, cumene, isopropylbenzene, meta-cleavage compound hydrolase, polychlorinated biphenyl degradation, Pseudomonas fluorescens IP01, alpha/beta-hydrolase, substrate specificity, cumene degradation, PCB, beta-ketolase, HYDROLASE ;; HYDROLASE
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.

1iuo__assembly_1__model_1

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

Download this curve (.dat)

1iuo__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

1iuo__assembly_1__model_1 | P(r) · Pending

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

Rg（Guinier）	26.57 Å
Rg (electron density)	25.80 Å
Total Rg	26.51 Å
Atom count	4310
Residues	544
Excluded volume	76183 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`1iuo__assembly_1__model_1`	dimeric （2）	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	meta-Cleavage product hydrolase
Molecular weight formula_weight	31506.6 kDa
EC 编号 ec_number	3.7.1.9
Mutation mutation	S103A
Source method src_method	man
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A
Atom count atom_count	2393

MANLEIGKSILAAGVLTNYHDVGEGQPVILIHGSGPGVSAYANWRLTIPALSKFYRVIAPDMVGFGFTDRPENYNYSKDSWVDHIIGIMDALEIEKAHIVGNAFGGGLAIATALRYSERVDRMVLMGAAGTRFDVTEGLNAVWGYTPSIENMRNLLDIFAYDRSLVTDELARLRYEASIQPGFQESFSSMFPEPRQRWIDALASSDEDIKTLPNETLIIHGREDQVVPLSSSLRLGELIDRAQLHVFGRCGHWTQIEQTDRFNRLVVEFFNEANTPKLVGRP

Source Source

Source organism organism	Pseudomonas fluorescens
NCBI taxonomy ID ncbi_taxonomy_id	294
Host organism host_organism	Escherichia coli

Entity 2 Entity 2 non-polymer

Description description	ACETATE ION
Molecular weight formula_weight	59.0 kDa
Source method src_method	syn
Copy count entity_count	2

Entity 3 Entity 3 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	238

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6. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_id	d1iuoa_
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.69 — alpha/beta-Hydrolases
Superfamily Superfamily superfamily	c.69.1 — alpha/beta-Hydrolases
Family Family family	c.69.1.10 — Carbon-carbon bond hydrolase

CATH v4.4 (1 domains)

Domain ID domain_id	1iuoA00
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	50 — Rossmann fold
Homologous superfamily homologous superfamily	1820 — Alpha/Beta hydrolase fold, catalytic domain

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Unit-cell length a length_a	76.543 Å
Unit-cell length b length_b	116.619 Å
Unit-cell length c length_c	78.037 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	C 2 2 21
Space-group number int_tables_number	20
Crystal system crystal_system	—

Resolution resolution	2.000 Å
Low-resolution limit resolution_low	29.600 Å
R factor r_factor	0.1759
R_work r_work	0.1740
R_free r_free	0.2110

meta-Cleavage product hydrolase from Pseudomonas fluorescens IP01 (CumD) S103A mutant complexed with acetates

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

meta-Cleavage product hydrolase

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

1iuo__assembly_1__model_1

1iuo__assembly_1__model_1 | I(q)

1iuo__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) 2 domains

SCOP 2.08 (1 domains)

CATH v4.4 (1 domains)

7. Citations (3)

meta-Cleavage product hydrolase from Pseudomonas fluorescens IP01 (CumD) S103A mutant complexed with acetates

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

meta-Cleavage product hydrolase

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

1iuo__assembly_1__model_1

1iuo__assembly_1__model_1 | I(q)

1iuo__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) 2 domains

SCOP 2.08 (1 domains)

CATH v4.4 (1 domains)

7. Citations (3)