SAXSdb — 2es4

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

Lipase

OrganismNot specified

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 2	Lipase chaperone × 1 （Q05490） CALCIUM ION × 1 IODIDE ION × 1 water × 2	Consistent with protein count
2	Protein heterocomplex	Heteromer	Protein 2	Lipase chaperone × 1 （Q05490） CALCIUM ION × 1 IODIDE ION × 7 water × 2	Consistent with protein count
3	Protein heterocomplex	Heteromer	Protein 8	Lipase chaperone × 4 （Q05490） CALCIUM ION × 4 IODIDE ION × 16 water × 8	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	LIP_BURGL
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–319； UniProt 40–358 Author chain B； PDBConstruct 1–319； UniProt 40–358

Lipase chaperone

Burkholderia glumae

UniProt Q05490

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 2	Lipase × 1 （Q05489） CALCIUM ION × 1 IODIDE ION × 1 water × 2	Consistent with protein count
2	Protein heterocomplex	Heteromer	Protein 2	Lipase × 1 （Q05489） CALCIUM ION × 1 IODIDE ION × 7 water × 2	Consistent with protein count
3	Protein heterocomplex	Heteromer	Protein 8	Lipase × 4 （Q05489） CALCIUM ION × 4 IODIDE ION × 16 water × 8	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	LIFO_BURGL
Isoform	—
PDB entities	2
Chains and sequence ranges	Author chain D； PDBConstruct 22–332； UniProt 42–353 Author chain E； PDBConstruct 22–332； UniProt 42–353

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	2es4
Deposition date deposition_date	2005-10-25
Structure title title	Crystal structure of the Burkholderia glumae lipase-specific foldase in complex with its cognate lipase
Keywords keywords	;protein-protein complex, steric chaperone, triacylglycerol hydrolase, all alpha helix protein, a/b hydrolase fold, extensive interaction area, 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.

2es4__assembly_1__model_1

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

Download this curve (.dat)

2es4__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

2es4__assembly_1__model_1 | P(r) · Pending

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

Rg（Guinier）	25.38 Å
Rg (electron density)	24.35 Å
Total Rg	25.29 Å
Atom count	4297
Residues	585
Excluded volume	75400 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`2es4__assembly_1__model_1`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
2	1	`2es4__assembly_2__model_1`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
3	1	`2es4__assembly_3__model_1`	octameric （8）	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 (5)

Entity 1 Entity 1 polymer

Description description	Lipase
Molecular weight formula_weight	33117.7 kDa
EC 编号 ec_number	3.1.1.3
Source method src_method	nat
Copy count entity_count	2

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B
Atom count atom_count	9463

ADTYAATRYPVILVHGLAGTDKFANVVDYWYGIQSDLQSHGAKVYVANLSGFQSDDGPNGRGEQLLAYVKQVLAATGATKVNLIGHSQGGLTSRYVAAVAPQLVASVTTIGTPHRGSEFADFVQDVLKTDPTGLSSTVIAAFVNVFGTLVSSSHNTDQDALAALRTLTTAQTATYNRNFPSAGLGAPGSCQTGAATETVGGSQHLLYSWGGTAIQPTSTVLGVTGATDTSTGTLDVANVTDPSTLALLATGAVMINRASGQNDGLVSRCSSLFGQVISTSYHWNHLDEINQLLGVRGANAEDPVAVIRTHVNRLKLQGV

Entity 2 Entity 2 polymer

Description description	Lipase chaperone
Molecular weight formula_weight	35236.2 kDa
Source method src_method	man
Copy count entity_count	2

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	D,E

GHHHHHHHHHHSSGHIEGRHMPAAPSPAPAGAVAGGPAAGVPAAASGAAEAAMPLPAALPGALAGSHAPRLPLAAGGRLARTRAVREFFDYCLTAQGELTPAALDALVRREIAAQLDGSPAQAEALGVWRRYRAYFDALAQLPGDGAVLGDKLDPAAMQLALDQRAALADRTLGEWAEPFFGDEQRRQRHDLERIRIANDTTLSPEQKAARLAALDAQLTPDERAQQAALHAQQDAVTKIADLQKAGATPDQMRAQIAQTLGPEAAARAAQMQQDDEAWQTRYQAYAAERDRIAAQGLAPQDRDARIAQLRQQTFTAPGEAIRAASLDRGAG

Source Source

Source organism organism	Burkholderia glumae
NCBI taxonomy ID ncbi_taxonomy_id	337
Host organism host_organism	Escherichia coli

Entity 3 Entity 3 non-polymer

Description description	CALCIUM ION
Molecular weight formula_weight	40.1 kDa
Source method src_method	syn
Copy count entity_count	2

Entity 4 Entity 4 non-polymer

Description description	IODIDE ION
Molecular weight formula_weight	126.9 kDa
Source method src_method	syn
Copy count entity_count	8

Entity 5 Entity 5 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	843

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6. Fold Classification (SCOP + CATH) 6 domains

SCOP 2.08 (4 domains)

Domain ID domain_id	d2es4a_
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.69.1.18 — Bacterial lipase

Domain ID domain_id	d2es4b_
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.69.1.18 — Bacterial lipase

Domain ID domain_id	d2es4d1
Class class	a — All alpha proteins
Fold Fold fold	a.137 — Non-globular all-alpha subunits of globular proteins
Superfamily Superfamily superfamily	a.137.15 — Lipase chaperone-like
Family Family family	a.137.15.1 — Lipase chaperone LifO-like

Domain ID domain_id	d2es4e_
Class class	a — All alpha proteins
Fold Fold fold	a.137 — Non-globular all-alpha subunits of globular proteins
Superfamily Superfamily superfamily	a.137.15 — Lipase chaperone-like
Family Family family	a.137.15.1 — Lipase chaperone LifO-like

CATH v4.4 (2 domains)

Domain ID domain_id	2es4A00
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	2es4B00
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	183.000 Å
Unit-cell length b length_b	75.700 Å
Unit-cell length c length_c	116.600 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	117.60 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	8

Space group space_group	C 1 2 1
Space-group number int_tables_number	5
Crystal system crystal_system	—

Resolution resolution	1.850 Å
Low-resolution limit resolution_low	40.000 Å
R factor r_factor	—
R_work r_work	0.1990
R_free r_free	0.2190

Crystal structure of the Burkholderia glumae lipase-specific foldase in complex with its cognate lipase

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

Lipase

State in the Current Structure

Other States of the Same Protein in the Database

Lipase chaperone

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

2es4__assembly_1__model_1

2es4__assembly_1__model_1 | I(q)

2es4__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 (5)

Entity 1 Entity 1 polymer

Polymer Polymer

Entity 2 Entity 2 polymer

Polymer Polymer

Source Source

Entity 3 Entity 3 non-polymer

Entity 4 Entity 4 non-polymer

Entity 5 Entity 5 water

6. Fold Classification (SCOP + CATH) 6 domains

SCOP 2.08 (4 domains)

CATH v4.4 (2 domains)

7. Citations (2)

Crystal structure of the Burkholderia glumae lipase-specific foldase in complex with its cognate lipase

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

Lipase

State in the Current Structure

Other States of the Same Protein in the Database

Monomer

Homodimer

Homotetramer

Other homooligomers

Heteromeric or nucleic-acid complex

Lipase chaperone

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

2es4__assembly_1__model_1

2es4__assembly_1__model_1 | I(q)

2es4__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 (5)

Entity 1 Entity 1 polymer

Polymer Polymer

Entity 2 Entity 2 polymer

Polymer Polymer

Source Source

Entity 3 Entity 3 non-polymer

Entity 4 Entity 4 non-polymer

Entity 5 Entity 5 water

6. Fold Classification (SCOP + CATH) 6 domains

SCOP 2.08 (4 domains)

CATH v4.4 (2 domains)

7. Citations (2)