3dd5

Glomerella cingulata E600-cutinase complex

Method: X-RAY DIFFRACTION

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

Cutinase

Glomerella cingulata

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein monomer	Monomer	Protein 1	DIETHYL PHOSPHONATE × 1 water × 1	Consistent with protein count
10	Protein homooligomer	Homooligomer	Protein 4	DIETHYL PHOSPHONATE × 4 water × 2	Consistent with protein count
11	Protein homooligomer	Homooligomer	Protein 2	DIETHYL PHOSPHONATE × 2 water × 1	Consistent with protein count
12	Protein homooligomer	Homooligomer	Protein 2	DIETHYL PHOSPHONATE × 2 water × 1	Consistent with protein count
13	Protein homooligomer	Homooligomer	Protein 2	DIETHYL PHOSPHONATE × 2 water × 1	Consistent with protein count
14	Protein homooligomer	Homooligomer	Protein 2	DIETHYL PHOSPHONATE × 2 water × 1	Consistent with protein count
2	Protein monomer	Monomer	Protein 1	DIETHYL PHOSPHONATE × 1	Consistent with protein count
3	Protein monomer	Monomer	Protein 1	DIETHYL PHOSPHONATE × 1 water × 1	Consistent with protein count
4	Protein monomer	Monomer	Protein 1	DIETHYL PHOSPHONATE × 1 water × 1	Consistent with protein count
5	Protein monomer	Monomer	Protein 1	DIETHYL PHOSPHONATE × 1	Consistent with protein count
6	Protein monomer	Monomer	Protein 1	DIETHYL PHOSPHONATE × 1	Consistent with protein count
7	Protein monomer	Monomer	Protein 1	DIETHYL PHOSPHONATE × 1	Consistent with protein count
8	Protein monomer	Monomer	Protein 1	DIETHYL PHOSPHONATE × 1 water × 1	Consistent with protein count
9	Protein homooligomer	Homooligomer	Protein 4	DIETHYL PHOSPHONATE × 4 water × 2	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	CUTI_COLGL
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 8–201； UniProt 31–224 Author chain B； PDBConstruct 8–201； UniProt 31–224 Author chain C； PDBConstruct 8–201； UniProt 31–224 Author chain D； PDBConstruct 8–201； UniProt 31–224 Author chain E； PDBConstruct 8–201； UniProt 31–224 Author chain F； PDBConstruct 8–201； UniProt 31–224 Author chain G； PDBConstruct 8–201； UniProt 31–224 Author chain H； PDBConstruct 8–201； UniProt 31–224

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	3dd5
Deposition date deposition_date	2008-06-05
Structure title title	Glomerella cingulata E600-cutinase complex
Keywords keywords	catalytic triad, Hydrolase, Secreted, Serine esterase; 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.

3dd5__assembly_1__model_1

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

Download this curve (.dat)

3dd5__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

3dd5__assembly_1__model_1 | P(r) · Pending

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

Rg（Guinier）	16.23 Å
Rg (electron density)	15.13 Å
Total Rg	16.29 Å
Atom count	1439
Residues	194
Excluded volume	25615 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`3dd5__assembly_1__model_1`	monomeric （1）	Success	4.1.3-1-20251215 (887e7ef)	View Download
2	1	`3dd5__assembly_2__model_1`	monomeric （1）	Success	4.1.3-1-20251215 (887e7ef)	View Download
3	1	`3dd5__assembly_3__model_1`	monomeric （1）	Success	4.1.3-1-20251215 (887e7ef)	View Download
4	1	`3dd5__assembly_4__model_1`	monomeric （1）	Success	4.1.3-1-20251215 (887e7ef)	View Download
5	1	`3dd5__assembly_5__model_1`	monomeric （1）	Success	4.1.3-1-20251215 (887e7ef)	View Download
6	1	`3dd5__assembly_6__model_1`	monomeric （1）	Success	4.1.3-1-20251215 (887e7ef)	View Download
7	1	`3dd5__assembly_7__model_1`	monomeric （1）	Success	4.1.3-1-20251215 (887e7ef)	View Download
8	1	`3dd5__assembly_8__model_1`	monomeric （1）	Success	4.1.3-1-20251215 (887e7ef)	View Download
9	1	`3dd5__assembly_9__model_1`	tetrameric （4）	Success	4.1.3-1-20251215 (887e7ef)	View Download
10	1	`3dd5__assembly_10__model_1`	tetrameric （4）	Success	4.1.3-1-20251215 (887e7ef)	View Download
11	1	`3dd5__assembly_11__model_1`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
12	1	`3dd5__assembly_12__model_1`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
13	1	`3dd5__assembly_13__model_1`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
14	1	`3dd5__assembly_14__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	Cutinase
Molecular weight formula_weight	21094.8 kDa
EC 编号 ec_number	3.1.1.74
Source method src_method	man
Copy count entity_count	8

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B,C,D,E,F,G,H
Atom count atom_count	11496

AMAISDPQSSTRNELETGSSSACPKVIYIFARASTEPGNMGISAGPIVADALERIYGANDVWVQGVGGPYLADLASNFLPDGTSSAAINEARRLFTLANTKCPNAAIVSGGYSQGTAVMAGSISGLSTTIKNQIKGVVLFGYTKNLQNLGRIPNFETSKTEVYCDIADAVCYGTLFILPAHFLYQTDAAVAAPRFLQARIG

Source Source

Source organism organism	Glomerella cingulata
Common name common_name	Anthracnose fungus
NCBI taxonomy ID ncbi_taxonomy_id	5457
Host organism host_organism	Escherichia coli

Entity 2 Entity 2 non-polymer

Description description	DIETHYL PHOSPHONATE
Molecular weight formula_weight	138.1 kDa
Source method src_method	syn
Copy count entity_count	8

Entity 3 Entity 3 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	4

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6. Fold Classification (SCOP + CATH) 16 domains

SCOP 2.08 (8 domains)

Domain ID domain_id	d3dd5a_
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.69.1.0 — automated matches

Domain ID domain_id	d3dd5b_
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.69.1.0 — automated matches

Domain ID domain_id	d3dd5c_
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.69.1.0 — automated matches

Domain ID domain_id	d3dd5d_
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.69.1.0 — automated matches

Domain ID domain_id	d3dd5e_
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.69.1.0 — automated matches

Domain ID domain_id	d3dd5f_
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.69.1.0 — automated matches

Domain ID domain_id	d3dd5g_
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.69.1.0 — automated matches

Domain ID domain_id	d3dd5h_
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.69.1.0 — automated matches

CATH v4.4 (8 domains)

Domain ID domain_id	3dd5A00
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

Domain ID domain_id	3dd5B00
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

Domain ID domain_id	3dd5C00
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

Domain ID domain_id	3dd5D00
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

Domain ID domain_id	3dd5E00
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

Domain ID domain_id	3dd5F00
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

Domain ID domain_id	3dd5G00
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

Domain ID domain_id	3dd5H00
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	73.470 Å
Unit-cell length b length_b	117.370 Å
Unit-cell length c length_c	95.240 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	103.57 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	16

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

Resolution resolution	2.600 Å
Low-resolution limit resolution_low	19.800 Å
R factor r_factor	0.2190
R_work r_work	0.2150
R_free r_free	0.2790

Glomerella cingulata E600-cutinase complex

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

Cutinase

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

3dd5__assembly_1__model_1

3dd5__assembly_1__model_1 | I(q)

3dd5__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) 16 domains

SCOP 2.08 (8 domains)

CATH v4.4 (8 domains)

7. Citations (1)

Glomerella cingulata E600-cutinase complex

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

Cutinase

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

3dd5__assembly_1__model_1

3dd5__assembly_1__model_1 | I(q)

3dd5__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) 16 domains

SCOP 2.08 (8 domains)

CATH v4.4 (8 domains)

7. Citations (1)