1m5y

Crystallographic Structure of SurA, a Molecular Chaperone that Facilitates Outer Membrane Porin Folding

Method: X-RAY DIFFRACTION

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

Survival protein surA

Escherichia coli

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein homooligomer	Homooligomer	Protein 4	No other associated polymer	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	SURA_ECOLI
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–408； UniProt 21–428 Author chain B； PDBConstruct 1–408； UniProt 21–428 Author chain C； PDBConstruct 1–408； UniProt 21–428 Author chain D； PDBConstruct 1–408； UniProt 21–428

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	1m5y
Deposition date deposition_date	2002-07-10
Structure title title	Crystallographic Structure of SurA, a Molecular Chaperone that Facilitates Outer Membrane Porin Folding
Keywords keywords	Survival protein A, periplasmic molecular chaperone, membrane protein folding, gram negative bacteria, ISOMERASE, CELL CYCLE; ISOMERASE, CELL CYCLE
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.

1m5y__assembly_1__model_1

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

Download this curve (.dat)

1m5y__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

1m5y__assembly_1__model_1 | P(r) · Pending

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

Rg（Guinier）	55.33 Å
Rg (electron density)	56.10 Å
Total Rg	55.77 Å
Atom count	11914
Residues	1530
Excluded volume	210570 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`1m5y__assembly_1__model_1`	tetrameric （4）	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 (1)

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6. Fold Classification (SCOP + CATH) 24 domains

SCOP 2.08 (12 domains)

Domain ID domain_id	d1m5ya1
Class class	a — All alpha proteins
Fold Fold fold	a.223 — Triger factor/SurA peptide-binding domain-like
Superfamily Superfamily superfamily	a.223.1 — Triger factor/SurA peptide-binding domain-like
Family Family family	a.223.1.2 — Porin chaperone SurA, peptide-binding domain

Domain ID domain_id	d1m5ya2
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.26 — FKBP-like
Superfamily Superfamily superfamily	d.26.1 — FKBP-like
Family Family family	d.26.1.1 — FKBP immunophilin/proline isomerase

Domain ID domain_id	d1m5ya3
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.26 — FKBP-like
Superfamily Superfamily superfamily	d.26.1 — FKBP-like
Family Family family	d.26.1.1 — FKBP immunophilin/proline isomerase

Domain ID domain_id	d1m5yb1
Class class	a — All alpha proteins
Fold Fold fold	a.223 — Triger factor/SurA peptide-binding domain-like
Superfamily Superfamily superfamily	a.223.1 — Triger factor/SurA peptide-binding domain-like
Family Family family	a.223.1.2 — Porin chaperone SurA, peptide-binding domain

Domain ID domain_id	d1m5yb2
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.26 — FKBP-like
Superfamily Superfamily superfamily	d.26.1 — FKBP-like
Family Family family	d.26.1.1 — FKBP immunophilin/proline isomerase

Domain ID domain_id	d1m5yb3
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.26 — FKBP-like
Superfamily Superfamily superfamily	d.26.1 — FKBP-like
Family Family family	d.26.1.1 — FKBP immunophilin/proline isomerase

Domain ID domain_id	d1m5yc1
Class class	a — All alpha proteins
Fold Fold fold	a.223 — Triger factor/SurA peptide-binding domain-like
Superfamily Superfamily superfamily	a.223.1 — Triger factor/SurA peptide-binding domain-like
Family Family family	a.223.1.2 — Porin chaperone SurA, peptide-binding domain

Domain ID domain_id	d1m5yc2
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.26 — FKBP-like
Superfamily Superfamily superfamily	d.26.1 — FKBP-like
Family Family family	d.26.1.1 — FKBP immunophilin/proline isomerase

Domain ID domain_id	d1m5yc3
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.26 — FKBP-like
Superfamily Superfamily superfamily	d.26.1 — FKBP-like
Family Family family	d.26.1.1 — FKBP immunophilin/proline isomerase

Domain ID domain_id	d1m5yd1
Class class	a — All alpha proteins
Fold Fold fold	a.223 — Triger factor/SurA peptide-binding domain-like
Superfamily Superfamily superfamily	a.223.1 — Triger factor/SurA peptide-binding domain-like
Family Family family	a.223.1.2 — Porin chaperone SurA, peptide-binding domain

Domain ID domain_id	d1m5yd2
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.26 — FKBP-like
Superfamily Superfamily superfamily	d.26.1 — FKBP-like
Family Family family	d.26.1.1 — FKBP immunophilin/proline isomerase

Domain ID domain_id	d1m5yd3
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.26 — FKBP-like
Superfamily Superfamily superfamily	d.26.1 — FKBP-like
Family Family family	d.26.1.1 — FKBP immunophilin/proline isomerase

CATH v4.4 (12 domains)

Domain ID domain_id	1m5yA01
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	4030 — Triger factor/SurA peptide-binding fold
Homologous superfamily homologous superfamily	10 — Porin chaperone SurA, peptide-binding domain

Domain ID domain_id	1m5yA02
Class class	3 — Alpha Beta
Architecture architecture	10 — Roll
Topology topology	50 — Chitinase A; domain 3
Homologous superfamily homologous superfamily	40 —

Domain ID domain_id	1m5yA03
Class class	3 — Alpha Beta
Architecture architecture	10 — Roll
Topology topology	50 — Chitinase A; domain 3
Homologous superfamily homologous superfamily	40 —

Domain ID domain_id	1m5yB01
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	4030 — Triger factor/SurA peptide-binding fold
Homologous superfamily homologous superfamily	10 — Porin chaperone SurA, peptide-binding domain

Domain ID domain_id	1m5yB02
Class class	3 — Alpha Beta
Architecture architecture	10 — Roll
Topology topology	50 — Chitinase A; domain 3
Homologous superfamily homologous superfamily	40 —

Domain ID domain_id	1m5yB03
Class class	3 — Alpha Beta
Architecture architecture	10 — Roll
Topology topology	50 — Chitinase A; domain 3
Homologous superfamily homologous superfamily	40 —

Domain ID domain_id	1m5yC01
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	4030 — Triger factor/SurA peptide-binding fold
Homologous superfamily homologous superfamily	10 — Porin chaperone SurA, peptide-binding domain

Domain ID domain_id	1m5yC02
Class class	3 — Alpha Beta
Architecture architecture	10 — Roll
Topology topology	50 — Chitinase A; domain 3
Homologous superfamily homologous superfamily	40 —

Domain ID domain_id	1m5yC03
Class class	3 — Alpha Beta
Architecture architecture	10 — Roll
Topology topology	50 — Chitinase A; domain 3
Homologous superfamily homologous superfamily	40 —

Domain ID domain_id	1m5yD01
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	4030 — Triger factor/SurA peptide-binding fold
Homologous superfamily homologous superfamily	10 — Porin chaperone SurA, peptide-binding domain

Domain ID domain_id	1m5yD02
Class class	3 — Alpha Beta
Architecture architecture	10 — Roll
Topology topology	50 — Chitinase A; domain 3
Homologous superfamily homologous superfamily	40 —

Domain ID domain_id	1m5yD03
Class class	3 — Alpha Beta
Architecture architecture	10 — Roll
Topology topology	50 — Chitinase A; domain 3
Homologous superfamily homologous superfamily	40 —

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Unit-cell length a length_a	158.817 Å
Unit-cell length b length_b	223.406 Å
Unit-cell length c length_c	279.721 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	64

Space group space_group	F 2 2 2
Space-group number int_tables_number	22
Crystal system crystal_system	—

Resolution resolution	3.000 Å
Low-resolution limit resolution_low	29.800 Å
R factor r_factor	0.2280
R_work r_work	0.2280
R_free r_free	0.2830

Description description	Survival protein surA
Molecular weight formula_weight	45131.9 kDa
EC 编号 ec_number	5.2.1.8
Source method src_method	man
Copy count entity_count	4

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B,C,D
Atom count atom_count	11914

Crystallographic Structure of SurA, a Molecular Chaperone that Facilitates Outer Membrane Porin Folding

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

Survival protein surA

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

1m5y__assembly_1__model_1

1m5y__assembly_1__model_1 | I(q)

1m5y__assembly_1__model_1 | P(r) · Pending

4. Crystallography and Experiment 4. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

Refinement Refinement

5. Entities and Polymers Entities & Polymers (1)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

6. Fold Classification (SCOP + CATH) 24 domains

SCOP 2.08 (12 domains)

CATH v4.4 (12 domains)

7. Citations (1)

Source organism organism	Escherichia coli
NCBI taxonomy ID ncbi_taxonomy_id	562
Host organism host_organism	Escherichia coli BL21(DE3)

Crystallographic Structure of SurA, a Molecular Chaperone that Facilitates Outer Membrane Porin Folding

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

Survival protein surA

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

1m5y__assembly_1__model_1

1m5y__assembly_1__model_1 | I(q)

1m5y__assembly_1__model_1 | P(r) · Pending

4. Crystallography and Experiment 4. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

Refinement Refinement

5. Entities and Polymers Entities & Polymers (1)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

6. Fold Classification (SCOP + CATH) 24 domains

SCOP 2.08 (12 domains)

CATH v4.4 (12 domains)

7. Citations (1)