SAXSdb — 1itx

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

Glycosyl Hydrolase

Bacillus circulans

UniProt P20533

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein monomer	Monomer	Protein 1	GLYCEROL × 11 water × 1	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	CHIA1_BACCI
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–419； UniProt 33–451

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	1itx
Deposition date deposition_date	2002-02-13
Structure title title	Catalytic Domain of Chitinase A1 from Bacillus circulans WL-12
Keywords keywords	Alpha-Beta (TIM) Barrel, 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.

1itx__assembly_1__model_1

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

Download this curve (.dat)

1itx__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

1itx__assembly_1__model_1 | P(r) · Pending

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

Rg（Guinier）	22.21 Å
Rg (electron density)	21.05 Å
Total Rg	22.04 Å
Atom count	3287
Residues	419
Excluded volume	57907 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`1itx__assembly_1__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	Glycosyl Hydrolase
Molecular weight formula_weight	45529.2 kDa
EC 编号 ec_number	3.2.1.14
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	4354

LQPATAEAADSYKIVGYYPSWAAYGRNYNVADIDPTKVTHINYAFADICWNGIHGNPDPSGPNPVTWTCQNEKSQTINVPNGTIVLGDPWIDTGKTFAGDTWDQPIAGNINQLNKLKQTNPNLKTIISVGGWTWSNRFSDVAATAATREVFANSAVDFLRKYNFDGVDLDWEYPVSGGLDGNSKRPEDKQNYTLLLSKIREKLDAAGAVDGKKYLLTIASGASATYAANTELAKIAAIVDWINIMTYDFNGAWQKISAHNAPLNYDPAASAAGVPDANTFNVAAGAQGHLDAGVPAAKLVLGVPFYGRGWDGCAQAGNGQYQTCTGGSSVGTWEAGSFDFYDLEANYINKNGYTRYWNDTAKVPYLYNASNKRFISYDDAESVGYKTAYIKSKGLGGAMFWELSGDRNKTLQNKLKADL

Source Source

Source organism organism	Bacillus circulans
NCBI taxonomy ID ncbi_taxonomy_id	1397
Host organism host_organism	Escherichia coli

Entity 2 Entity 2 non-polymer

Description description	GLYCEROL
Molecular weight formula_weight	92.1 kDa
Source method src_method	syn
Copy count entity_count	11

Entity 3 Entity 3 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	770

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6. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_id	d1itxa1
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.1 — TIM beta/alpha-barrel
Superfamily Superfamily superfamily	c.1.8 — (Trans)glycosidases
Family Family family	c.1.8.5 — Type II chitinase

Domain ID domain_id	d1itxa2
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.26 — FKBP-like
Superfamily Superfamily superfamily	d.26.3 — Chitinase insertion domain
Family Family family	d.26.3.1 — Chitinase insertion domain

CATH v4.4 (2 domains)

Domain ID domain_id	1itxA01
Class class	3 — Alpha Beta
Architecture architecture	20 — Alpha-Beta Barrel
Topology topology	20 — TIM Barrel
Homologous superfamily homologous superfamily	80 — Glycosidases

Domain ID domain_id	1itxA02
Class class	3 — Alpha Beta
Architecture architecture	10 — Roll
Topology topology	50 — Chitinase A; domain 3
Homologous superfamily homologous superfamily	10 —

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7. Citations (6)

Three-dimensional structure of the catalytic domain of chitinase A1 from Bacillus circulans WL-12 at a very high resolution

PROC.JPN.ACAD.,SER.B (1999)

PMID: -1 PRIMARY

;Trp122 and Trp134 on the surface of the catalytic domain are essential for crystalline chitin hydrolysis by Bacillus circulans chitinase A1 ;

FEBS LETT. (2001)

DOI: 10.1016/S0014-5793(01)02317-1

Roles of the exposed aromatic residues in crystalline chitin hydrolysis by chitinase A from Serratia marcescens 2170

J.BIOL.CHEM. (2001)

DOI: 10.1074/jbc.M103610200

Crystallization and A Preliminary Crystallographic Analysis of the Catalytic Domain of Chitinase Al from Bacillus Circulans WL-12

PROTEIN PEPT.LETT. (1999)

;Identification of glutamic acid 204 and aspartic acid 200 in chitinase A1 of Bacillus circulans WL-12 as essential residues for chitinase activity ;

J.BIOL.CHEM. (1993)

;Gene cloning of chitinase A1 from Bacillus circulans WL-12 revealed its evolutionary relationship to Serratia chitinase and to the type III homology units of fibronectin ;

J.BIOL.CHEM. (1990)

Unit-cell length a length_a	43.007 Å
Unit-cell length b length_b	46.839 Å
Unit-cell length c length_c	55.700 Å
Unit-cell angle α angle_alpha	109.29 °
Unit-cell angle β angle_beta	95.45 °
Unit-cell angle γ angle_gamma	116.68 °
Molecules per unit cell Z z_pdb	1

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

Resolution resolution	1.100 Å
Low-resolution limit resolution_low	36.793 Å
R factor r_factor	0.1173
R_work r_work	0.1163
R_free r_free	0.1372

Catalytic Domain of Chitinase A1 from Bacillus circulans WL-12

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

Glycosyl 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

1itx__assembly_1__model_1

1itx__assembly_1__model_1 | I(q)

1itx__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) 4 domains

SCOP 2.08 (2 domains)

CATH v4.4 (2 domains)

7. Citations (6)

Catalytic Domain of Chitinase A1 from Bacillus circulans WL-12

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

Glycosyl 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

1itx__assembly_1__model_1

1itx__assembly_1__model_1 | I(q)

1itx__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) 4 domains

SCOP 2.08 (2 domains)

CATH v4.4 (2 domains)

7. Citations (6)