SAXSdb — 3znc

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

CARBONIC ANHYDRASE IV

Mus musculus

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 × 2 (+)-4-ETHYLAMINO-3,4-DIHYDRO-2-(METHOXY)PROPYL-2H-THIENO[3,2-E]-1,2-THIAZINE-6-SULFONAMIDE-1,1-DIOXIDE × 2 water × 2	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	CAH4_MOUSE
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–258； UniProt 22–279

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	3znc
Deposition date deposition_date	1998-02-10
Structure title title	MURINE CARBONIC ANHYDRASE IV COMPLEXED WITH BRINZOLAMIDE
Keywords keywords	LYASE, ZINC, MURINE, MEMBRANE, INHIBITOR; 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.

3znc__assembly_1__model_1

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

Download this curve (.dat)

3znc__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

3znc__assembly_1__model_1 | P(r) · Pending

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

Rg（Guinier）	28.06 Å
Rg (electron density)	27.18 Å
Total Rg	27.81 Å
Atom count	4994
Residues	500
Excluded volume	72289 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`3znc__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 (4)

Entity 1 Entity 1 polymer

Description description	CARBONIC ANHYDRASE IV
Molecular weight formula_weight	29490.5 kDa
EC 编号 ec_number	4.2.1.1
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	2499

WCYEIQTEDPRSSCLGPEKWPGACKENQQSPINIVTARTKVNPRLTPFILVGYDQKQQWPIKNNQHTVEMTLGGGACIIGGDLPARYEAVQLHLHWSNGNDNGSEHSIDGRHFAMEMHIVHKKLTSSKEDSKDKFAVLAFMIEVGDKVNKGFQPLVEALPSISKPHSTSTVRESSLQDMLPPSTKMYTYFRYNGSLTTPNCDETVIWTVYKQPIKIHKNQFLEFSKNLYYDEDQKLNMKDNVRPLQPLGKRQVFKSHA

Source Source

Source organism organism	Mus musculus
Common name common_name	house mouse
NCBI taxonomy ID ncbi_taxonomy_id	10090
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	1

Entity 3 Entity 3 non-polymer

Description description	(+)-4-ETHYLAMINO-3,4-DIHYDRO-2-(METHOXY)PROPYL-2H-THIENO[3,2-E]-1,2-THIAZINE-6-SULFONAMIDE-1,1-DIOXIDE
Molecular weight formula_weight	383.5 kDa
Source method src_method	syn
Copy count entity_count	1

Entity 4 Entity 4 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	2

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6. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_id	d3znca_
Class class	b — All beta proteins
Fold Fold fold	b.74 — Carbonic anhydrase
Superfamily Superfamily superfamily	b.74.1 — Carbonic anhydrase
Family Family family	b.74.1.1 — Carbonic anhydrase

CATH v4.4 (1 domains)

Domain ID domain_id	3zncA00
Class class	3 — Alpha Beta
Architecture architecture	10 — Roll
Topology topology	200 — Carbonic Anhydrase II
Homologous superfamily homologous superfamily	10 — Alpha carbonic anhydrase

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Unit-cell length a length_a	53.500 Å
Unit-cell length b length_b	85.200 Å
Unit-cell length c length_c	121.900 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	2.800 Å
Low-resolution limit resolution_low	20.000 Å
R factor r_factor	0.1910
R_work r_work	0.1910
R_free r_free	0.2770

MURINE CARBONIC ANHYDRASE IV COMPLEXED WITH BRINZOLAMIDE

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

CARBONIC ANHYDRASE IV

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

3znc__assembly_1__model_1

3znc__assembly_1__model_1 | I(q)

3znc__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) 2 domains

SCOP 2.08 (1 domains)

CATH v4.4 (1 domains)

7. Citations (2)

MURINE CARBONIC ANHYDRASE IV COMPLEXED WITH BRINZOLAMIDE

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

CARBONIC ANHYDRASE IV

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

3znc__assembly_1__model_1

3znc__assembly_1__model_1 | I(q)

3znc__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) 2 domains

SCOP 2.08 (1 domains)

CATH v4.4 (1 domains)

7. Citations (2)