SAXSdb — 4lp6

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

Carbonic anhydrase 2

Homo sapiens

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein monomer	Monomer	Protein 1	;8-({[4-(3-aminopropoxy)-8-({[4-hydroxy-8-({[4-(2-methylpropoxy)-8-({[4-(3-{[(4-sulfamoylbenzoyl)amino]methyl}phenoxy)butyl]carbamoyl}amino)quinolin-2-yl]carbonyl}amino)quinolin-2-yl]carbonyl}amino)quinolin-2-yl]carbonyl}amino)-4-(carboxymethoxy)quinoline-2-carboxylic acid ; × 1 ZINC ION × 9 water × 1	Consistent with protein count
2	Protein monomer	Monomer	Protein 1	;8-({[4-(3-aminopropoxy)-8-({[4-hydroxy-8-({[4-(2-methylpropoxy)-8-({[4-(3-{[(4-sulfamoylbenzoyl)amino]methyl}phenoxy)butyl]carbamoyl}amino)quinolin-2-yl]carbonyl}amino)quinolin-2-yl]carbonyl}amino)quinolin-2-yl]carbonyl}amino)-4-(carboxymethoxy)quinoline-2-carboxylic acid ; × 1 ZINC ION × 4 water × 1	Consistent with protein count
3	Protein homooligomer	Homooligomer	Protein 2	;8-({[4-(3-aminopropoxy)-8-({[4-hydroxy-8-({[4-(2-methylpropoxy)-8-({[4-(3-{[(4-sulfamoylbenzoyl)amino]methyl}phenoxy)butyl]carbamoyl}amino)quinolin-2-yl]carbonyl}amino)quinolin-2-yl]carbonyl}amino)quinolin-2-yl]carbonyl}amino)-4-(carboxymethoxy)quinoline-2-carboxylic acid ; × 2 ZINC ION × 13 water × 2	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	CAH2_HUMAN
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–260； UniProt 1–260 Author chain B； PDBConstruct 1–260； UniProt 1–260

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	4lp6
Deposition date deposition_date	2013-07-15
Structure title title	Crystal Structure of Human Carbonic Anhydrase II in complex with a quinoline oligoamide foldamer
Keywords keywords	;protein-foldamer complex, protein foldamer interactions, modified inhibitor, anchored foldamer, HCAII dimerisation, Quinoline oligoamide foldamer, Benzene sulfonamide modified inhibitor, Lyase-lyase Inhibitor complex ;; Lyase/lyase Inhibitor
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.

4lp6__assembly_1__model_1

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

Download this curve (.dat)

4lp6__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

4lp6__assembly_1__model_1 | P(r) · Pending

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

Rg（Guinier）	18.80 Å
Rg (electron density)	17.41 Å
Total Rg	18.60 Å
Atom count	2081
Residues	257
Excluded volume	36809 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`4lp6__assembly_1__model_1`	monomeric （1）	Success	4.1.3-1-20251215 (887e7ef)	View Download
2	1	`4lp6__assembly_2__model_1`	monomeric （1）	Success	4.1.3-1-20251215 (887e7ef)	View Download
3	1	`4lp6__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	Carbonic anhydrase 2
Molecular weight formula_weight	29289.1 kDa
EC 编号 ec_number	4.2.1.1
Source method src_method	man
Copy count entity_count	2

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B
Atom count atom_count	4276

MSHHWGYGKHNGPEHWHKDFPIAKGERQSPVDIDTHTAKYDPSLKPLSVSYDQATSLRILNNGHAFNVEFDDSQDKAVLKGGPLDGTYRLIQFHFHWGSLDGQGSEHTVDKKKYAAELHLVHWNTKYGDFGKAVQQPDGLAVLGIFLKVGSAKPGLQKVVDVLDSIKTKGKSADFTNFDPRGLLPESLDYWTYPGSLTTPPLLECVTWIVLKEPISVSSEQVLKFRKLNFNGEGEPEELMVDNWRPAQPLKNRQIKASFK

Source Source

Source organism organism	Homo sapiens
Common name common_name	human
NCBI taxonomy ID ncbi_taxonomy_id	9606
Host organism host_organism	Escherichia coli

Entity 2 Entity 2 non-polymer

Description description	;8-({[4-(3-aminopropoxy)-8-({[4-hydroxy-8-({[4-(2-methylpropoxy)-8-({[4-(3-{[(4-sulfamoylbenzoyl)amino]methyl}phenoxy)butyl]carbamoyl}amino)quinolin-2-yl]carbonyl}amino)quinolin-2-yl]carbonyl}amino)quinolin-2-yl]carbonyl}amino)-4-(carboxymethoxy)quinoline-2-carboxylic acid ;
Molecular weight formula_weight	1337.4 kDa
Source method src_method	syn
Copy count entity_count	2

Entity 3 Entity 3 non-polymer

Description description	ZINC ION
Molecular weight formula_weight	65.4 kDa
Source method src_method	syn
Copy count entity_count	13

Entity 4 Entity 4 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	148

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6. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_id	d4lp6a_
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

Domain ID domain_id	d4lp6b_
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 (2 domains)

Domain ID domain_id	4lp6A00
Class class	3 — Alpha Beta
Architecture architecture	10 — Roll
Topology topology	200 — Carbonic Anhydrase II
Homologous superfamily homologous superfamily	10 — Alpha carbonic anhydrase

Domain ID domain_id	4lp6B00
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	45.960 Å
Unit-cell length b length_b	84.170 Å
Unit-cell length c length_c	76.700 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	97.18 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	4

Space group space_group	P 1 21 1
Space-group number int_tables_number	4
Crystal system crystal_system	—

Resolution resolution	2.150 Å
Low-resolution limit resolution_low	41.500 Å
R factor r_factor	0.1942
R_work r_work	0.1912
R_free r_free	0.2533

Crystal Structure of Human Carbonic Anhydrase II in complex with a quinoline oligoamide foldamer

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

Carbonic anhydrase 2

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

4lp6__assembly_1__model_1

4lp6__assembly_1__model_1 | I(q)

4lp6__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) 4 domains

SCOP 2.08 (2 domains)

CATH v4.4 (2 domains)

7. Citations (1)

Crystal Structure of Human Carbonic Anhydrase II in complex with a quinoline oligoamide foldamer

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

Carbonic anhydrase 2

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

4lp6__assembly_1__model_1

4lp6__assembly_1__model_1 | I(q)

4lp6__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) 4 domains

SCOP 2.08 (2 domains)

CATH v4.4 (2 domains)

7. Citations (1)