4av7

Structure determination of the double mutant S233Y F250G from the sec- alkyl sulfatase PisA1

Method: X-RAY DIFFRACTION

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

SEC-ALKYLSULFATASE

PSEUDOMONAS SP. DSM 6611

State in the Current Structure

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

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	F8KAY7_9PSED
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–660； UniProt 1–660 Author chain B； PDBConstruct 1–660； UniProt 1–660 Author chain C； PDBConstruct 1–660； UniProt 1–660 Author chain D； PDBConstruct 1–660； UniProt 1–660 Author chain E； PDBConstruct 1–660； UniProt 1–660 Author chain F； PDBConstruct 1–660； UniProt 1–660

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	4av7
Deposition date deposition_date	2012-05-24
Structure title title	Structure determination of the double mutant S233Y F250G from the sec- alkyl sulfatase PisA1
Keywords keywords	HYDROLASE, INVERTING ALKYLSULFATASE, DOUBLE MUTANT; 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.

4av7__assembly_1__model_1

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

Download this curve (.dat)

4av7__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

4av7__assembly_1__model_1 | P(r) · Pending

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

Rg（Guinier）	31.58 Å
Rg (electron density)	30.78 Å
Total Rg	31.55 Å
Atom count	9886
Residues	1268
Excluded volume	175540 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`4av7__assembly_1__model_1`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
2	1	`4av7__assembly_2__model_1`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
3	1	`4av7__assembly_3__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 (4)

Entity 1 Entity 1 polymer

Description description	SEC-ALKYLSULFATASE
Molecular weight formula_weight	73965.0 kDa
Mutation mutation	YES
Source method src_method	man
Copy count entity_count	6

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B,C,D,E,F
Atom count atom_count	30000

MSRFIRASQRRTLLATLIAATLAQPLLAAESLDSKPASAITAAKNAEVLKNLPFADREEFEAAKRGLIAPFSGQIKNAEGQVVWDMGAYQFLNDKDAADTVNPSLWRQAQLNNIAGLFEVMPKLYQVRGLDPANMTIIEGDSGLVLIDTLTTAETARAALDLYFQHRPKKPIVAVVYSHSHIDHFGGARGIIDEADVKAGKVKVFAPSGFMEHAVSENILAGTAMARRGQYQYGVMVPRGAQAQVDSGLGKTTATNATNTLVAPNVLIEKPYERHTVDGVELEFQLTLGSEAPSDMNIYLPQFKVLNTADNAPPAMHNLLTPRGAEVRDAKAWAGYIDASLEKYGDRTDVLIQQHNWPVWGGDKVRTYLADQRDMYAFLNNRALNLMNKGLTLHEIAAEVSKLPGELDRKWYLRSYYGALSTNLRAVYQRYLGFYDGNPANLDPFPPVEAGKRYVEAMGGADAVLKQMRAAIDKGDYRWAVQLGNHLVFADPANKDARALQADAMEQLGYQTENALWRNMYMTGAMELRHGVPTYDSRGKSEMGRALTPDMFFDLLAIRLDTDKAVGHDMTLNWVFEDLKQDIALTLRNGVLTQRVGSLNPKADVTVKLTKPTLDQIAARKLDLPTAIKQGTVKLDGDGKKLGEFFGLLDSFSPKFNIVELEHHHHHH

Source Source

Source organism organism	PSEUDOMONAS SP. DSM 6611
NCBI taxonomy ID ncbi_taxonomy_id	1007495
Host organism host_organism	ESCHERICHIA COLI

Entity 2 Entity 2 non-polymer

Description description	ZINC ION
Molecular weight formula_weight	65.4 kDa
Source method src_method	syn
Copy count entity_count	12

Entity 3 Entity 3 non-polymer

Description description	SULFATE ION
Molecular weight formula_weight	96.1 kDa
Source method src_method	syn
Copy count entity_count	6

Entity 4 Entity 4 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	318

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6. Fold Classification (SCOP + CATH) 36 domains

SCOP 2.08 (18 domains)

Domain ID domain_id	d4av7a1
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.157 — Metallo-hydrolase/oxidoreductase
Superfamily Superfamily superfamily	d.157.1 — Metallo-hydrolase/oxidoreductase
Family Family family	d.157.1.0 — automated matches

Domain ID domain_id	d4av7a2
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.106 — SCP-like
Superfamily Superfamily superfamily	d.106.1 — SCP-like
Family Family family	d.106.1.0 — automated matches

Domain ID domain_id	d4av7a3
Class class	l — Artifacts
Fold Fold fold	l.1 — Tags
Superfamily Superfamily superfamily	l.1.1 — Tags
Family Family family	l.1.1.1 — Tags

Domain ID domain_id	d4av7b1
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.157 — Metallo-hydrolase/oxidoreductase
Superfamily Superfamily superfamily	d.157.1 — Metallo-hydrolase/oxidoreductase
Family Family family	d.157.1.0 — automated matches

Domain ID domain_id	d4av7b2
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.106 — SCP-like
Superfamily Superfamily superfamily	d.106.1 — SCP-like
Family Family family	d.106.1.0 — automated matches

Domain ID domain_id	d4av7b3
Class class	l — Artifacts
Fold Fold fold	l.1 — Tags
Superfamily Superfamily superfamily	l.1.1 — Tags
Family Family family	l.1.1.1 — Tags

Domain ID domain_id	d4av7c1
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.157 — Metallo-hydrolase/oxidoreductase
Superfamily Superfamily superfamily	d.157.1 — Metallo-hydrolase/oxidoreductase
Family Family family	d.157.1.0 — automated matches

Domain ID domain_id	d4av7c2
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.106 — SCP-like
Superfamily Superfamily superfamily	d.106.1 — SCP-like
Family Family family	d.106.1.0 — automated matches

Domain ID domain_id	d4av7c3
Class class	l — Artifacts
Fold Fold fold	l.1 — Tags
Superfamily Superfamily superfamily	l.1.1 — Tags
Family Family family	l.1.1.1 — Tags

Domain ID domain_id	d4av7d1
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.157 — Metallo-hydrolase/oxidoreductase
Superfamily Superfamily superfamily	d.157.1 — Metallo-hydrolase/oxidoreductase
Family Family family	d.157.1.0 — automated matches

Domain ID domain_id	d4av7d2
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.106 — SCP-like
Superfamily Superfamily superfamily	d.106.1 — SCP-like
Family Family family	d.106.1.0 — automated matches

Domain ID domain_id	d4av7d3
Class class	l — Artifacts
Fold Fold fold	l.1 — Tags
Superfamily Superfamily superfamily	l.1.1 — Tags
Family Family family	l.1.1.1 — Tags

Domain ID domain_id	d4av7e1
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.157 — Metallo-hydrolase/oxidoreductase
Superfamily Superfamily superfamily	d.157.1 — Metallo-hydrolase/oxidoreductase
Family Family family	d.157.1.0 — automated matches

Domain ID domain_id	d4av7e2
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.106 — SCP-like
Superfamily Superfamily superfamily	d.106.1 — SCP-like
Family Family family	d.106.1.0 — automated matches

Domain ID domain_id	d4av7e3
Class class	l — Artifacts
Fold Fold fold	l.1 — Tags
Superfamily Superfamily superfamily	l.1.1 — Tags
Family Family family	l.1.1.1 — Tags

Domain ID domain_id	d4av7f1
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.157 — Metallo-hydrolase/oxidoreductase
Superfamily Superfamily superfamily	d.157.1 — Metallo-hydrolase/oxidoreductase
Family Family family	d.157.1.0 — automated matches

Domain ID domain_id	d4av7f2
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.106 — SCP-like
Superfamily Superfamily superfamily	d.106.1 — SCP-like
Family Family family	d.106.1.0 — automated matches

Domain ID domain_id	d4av7f3
Class class	l — Artifacts
Fold Fold fold	l.1 — Tags
Superfamily Superfamily superfamily	l.1.1 — Tags
Family Family family	l.1.1.1 — Tags

CATH v4.4 (18 domains)

Domain ID domain_id	4av7A01
Class class	3 — Alpha Beta
Architecture architecture	60 — 4-Layer Sandwich
Topology topology	15 — Metallo-beta-lactamase; Chain A
Homologous superfamily homologous superfamily	30 — Metallo-beta-lactamase domain

Domain ID domain_id	4av7A02
Class class	1 — Mainly Alpha
Architecture architecture	25 — Alpha Horseshoe
Topology topology	40 — Serine Threonine Protein Phosphatase 5, Tetratricopeptide repeat
Homologous superfamily homologous superfamily	880 — Alkyl sulfatase, dimerisation domain

Domain ID domain_id	4av7A03
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	1050 — Nonspecific Lipid-transfer Protein; Chain A
Homologous superfamily homologous superfamily	10 — SCP2 sterol-binding domain

Domain ID domain_id	4av7B01
Class class	3 — Alpha Beta
Architecture architecture	60 — 4-Layer Sandwich
Topology topology	15 — Metallo-beta-lactamase; Chain A
Homologous superfamily homologous superfamily	30 — Metallo-beta-lactamase domain

Domain ID domain_id	4av7B02
Class class	1 — Mainly Alpha
Architecture architecture	25 — Alpha Horseshoe
Topology topology	40 — Serine Threonine Protein Phosphatase 5, Tetratricopeptide repeat
Homologous superfamily homologous superfamily	880 — Alkyl sulfatase, dimerisation domain

Domain ID domain_id	4av7B03
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	1050 — Nonspecific Lipid-transfer Protein; Chain A
Homologous superfamily homologous superfamily	10 — SCP2 sterol-binding domain

Domain ID domain_id	4av7C01
Class class	3 — Alpha Beta
Architecture architecture	60 — 4-Layer Sandwich
Topology topology	15 — Metallo-beta-lactamase; Chain A
Homologous superfamily homologous superfamily	30 — Metallo-beta-lactamase domain

Domain ID domain_id	4av7C02
Class class	1 — Mainly Alpha
Architecture architecture	25 — Alpha Horseshoe
Topology topology	40 — Serine Threonine Protein Phosphatase 5, Tetratricopeptide repeat
Homologous superfamily homologous superfamily	880 — Alkyl sulfatase, dimerisation domain

Domain ID domain_id	4av7C03
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	1050 — Nonspecific Lipid-transfer Protein; Chain A
Homologous superfamily homologous superfamily	10 — SCP2 sterol-binding domain

Domain ID domain_id	4av7D01
Class class	3 — Alpha Beta
Architecture architecture	60 — 4-Layer Sandwich
Topology topology	15 — Metallo-beta-lactamase; Chain A
Homologous superfamily homologous superfamily	30 — Metallo-beta-lactamase domain

Domain ID domain_id	4av7D02
Class class	1 — Mainly Alpha
Architecture architecture	25 — Alpha Horseshoe
Topology topology	40 — Serine Threonine Protein Phosphatase 5, Tetratricopeptide repeat
Homologous superfamily homologous superfamily	880 — Alkyl sulfatase, dimerisation domain

Domain ID domain_id	4av7D03
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	1050 — Nonspecific Lipid-transfer Protein; Chain A
Homologous superfamily homologous superfamily	10 — SCP2 sterol-binding domain

Domain ID domain_id	4av7E01
Class class	3 — Alpha Beta
Architecture architecture	60 — 4-Layer Sandwich
Topology topology	15 — Metallo-beta-lactamase; Chain A
Homologous superfamily homologous superfamily	30 — Metallo-beta-lactamase domain

Domain ID domain_id	4av7E02
Class class	1 — Mainly Alpha
Architecture architecture	25 — Alpha Horseshoe
Topology topology	40 — Serine Threonine Protein Phosphatase 5, Tetratricopeptide repeat
Homologous superfamily homologous superfamily	880 — Alkyl sulfatase, dimerisation domain

Domain ID domain_id	4av7E03
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	1050 — Nonspecific Lipid-transfer Protein; Chain A
Homologous superfamily homologous superfamily	10 — SCP2 sterol-binding domain

Domain ID domain_id	4av7F01
Class class	3 — Alpha Beta
Architecture architecture	60 — 4-Layer Sandwich
Topology topology	15 — Metallo-beta-lactamase; Chain A
Homologous superfamily homologous superfamily	30 — Metallo-beta-lactamase domain

Domain ID domain_id	4av7F02
Class class	1 — Mainly Alpha
Architecture architecture	25 — Alpha Horseshoe
Topology topology	40 — Serine Threonine Protein Phosphatase 5, Tetratricopeptide repeat
Homologous superfamily homologous superfamily	880 — Alkyl sulfatase, dimerisation domain

Domain ID domain_id	4av7F03
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	1050 — Nonspecific Lipid-transfer Protein; Chain A
Homologous superfamily homologous superfamily	10 — SCP2 sterol-binding domain

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Unit-cell length a length_a	75.201 Å
Unit-cell length b length_b	201.955 Å
Unit-cell length c length_c	248.495 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	24

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

Resolution resolution	3.000 Å
Low-resolution limit resolution_low	45.650 Å
R factor r_factor	0.1900
R_work r_work	0.1865
R_free r_free	0.2559

Structure determination of the double mutant S233Y F250G from the sec- alkyl sulfatase PisA1

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

SEC-ALKYLSULFATASE

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

4av7__assembly_1__model_1

4av7__assembly_1__model_1 | I(q)

4av7__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 (4)

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 water

6. Fold Classification (SCOP + CATH) 36 domains

SCOP 2.08 (18 domains)

CATH v4.4 (18 domains)

7. Citations (1)

Structure determination of the double mutant S233Y F250G from the sec- alkyl sulfatase PisA1

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

SEC-ALKYLSULFATASE

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

4av7__assembly_1__model_1

4av7__assembly_1__model_1 | I(q)

4av7__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 (4)

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 water

6. Fold Classification (SCOP + CATH) 36 domains

SCOP 2.08 (18 domains)

CATH v4.4 (18 domains)

7. Citations (1)