SAXSdb — 3u1p

▼

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

Mycobacteria Tuberculosis LD-transpeptidase type 2

Mycobacterium tuberculosis

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein monomer	Monomer	Protein 1	DI(HYDROXYETHYL)ETHER × 1 water × 1	Consistent with protein count
2	Protein monomer	Monomer	Protein 1	DI(HYDROXYETHYL)ETHER × 1 water × 1	Consistent with protein count
3	Protein homooligomer	Homooligomer	Protein 2	DI(HYDROXYETHYL)ETHER × 2 water × 2	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	O53223_MYCTU
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–287； UniProt 122–408 Author chain B； PDBConstruct 1–287； UniProt 122–408

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.

▼

2. Structure Basics 2. Structure Basics

Entry ID entry_id	3u1p
Deposition date deposition_date	2011-09-30
Structure title title	Crystal Structure of M. tuberculosis LD-transpeptidase type 2 with Modified Catalytic Cysteine (C354)
Keywords keywords	protein-peptidoglycan complex, PEPTIDOGLYCAN BINDING PROTEIN; PEPTIDOGLYCAN BINDING PROTEIN
Experimental Method method	X-RAY DIFFRACTION

▼

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.

3u1p__assembly_1__model_1

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

Download this curve (.dat)

3u1p__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

3u1p__assembly_1__model_1 | P(r) · Pending

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

Rg（Guinier）	20.42 Å
Rg (electron density)	19.45 Å
Total Rg	20.30 Å
Atom count	2050
Residues	265
Excluded volume	35950 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`3u1p__assembly_1__model_1`	monomeric （1）	Success	4.1.3-1-20251215 (887e7ef)	View Download
2	1	`3u1p__assembly_2__model_1`	monomeric （1）	Success	4.1.3-1-20251215 (887e7ef)	View Download
3	1	`3u1p__assembly_3__model_1`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download

▶

4. Crystallography and Experiment 4. Crystallography & Experiment

▶

5. Entities and Polymers Entities & Polymers (3)

Entity 1 Entity 1 polymer

Description description	Mycobacteria Tuberculosis LD-transpeptidase type 2
Molecular weight formula_weight	31143.5 kDa
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	4244

RRYTLNATALGLGGAATRQLTFQTSSPAHLTMPYVMPGDGEVVGVGEPVAIRFDENIADRGAAEKAIKITTNPPVEGAFYWLNNREVRWRPEHFWKPGTAVDVAVNTYGVDLGEGMFGEDNVQTHFTIGDEVIATADDNTKILTVRVNGEVVKSMPTSMGKDSTPTANGIYIVGSRYKHIIMDSSTYGVPVNSPNGYRTDVDWATQISYSGVFVHSAPWSVGAQGHTNTSHGCLNVSPSNAQWFYDHVKRGDIVEVVNTVGGTLPGIDGLGDWNIPWDQWRAGNAKA

Source Source

Source organism organism	Mycobacterium tuberculosis
NCBI taxonomy ID ncbi_taxonomy_id	1773
Host organism host_organism	Escherichia coli

Entity 2 Entity 2 non-polymer

Description description	DI(HYDROXYETHYL)ETHER
Molecular weight formula_weight	106.1 kDa
Source method src_method	syn
Copy count entity_count	2

Entity 3 Entity 3 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	154

▼

6. Fold Classification (SCOP + CATH) 8 domains

SCOP 2.08 (4 domains)

Domain ID domain_id	d3u1pa1
Class class	b — All beta proteins
Fold Fold fold	b.1 — Immunoglobulin-like beta-sandwich
Superfamily Superfamily superfamily	b.1.18 — E set domains
Family Family family	b.1.18.24 — L,D-transpeptidase immunoglobulin-like domain

Domain ID domain_id	d3u1pa2
Class class	b — All beta proteins
Fold Fold fold	b.160 — L,D-transpeptidase catalytic domain-like
Superfamily Superfamily superfamily	b.160.1 — L,D-transpeptidase catalytic domain-like
Family Family family	b.160.1.1 — L,D-transpeptidase catalytic domain-like

Domain ID domain_id	d3u1pb1
Class class	b — All beta proteins
Fold Fold fold	b.1 — Immunoglobulin-like beta-sandwich
Superfamily Superfamily superfamily	b.1.18 — E set domains
Family Family family	b.1.18.24 — L,D-transpeptidase immunoglobulin-like domain

Domain ID domain_id	d3u1pb2
Class class	b — All beta proteins
Fold Fold fold	b.160 — L,D-transpeptidase catalytic domain-like
Superfamily Superfamily superfamily	b.160.1 — L,D-transpeptidase catalytic domain-like
Family Family family	b.160.1.1 — L,D-transpeptidase catalytic domain-like

CATH v4.4 (4 domains)

Domain ID domain_id	3u1pA01
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	40 — Immunoglobulin-like
Homologous superfamily homologous superfamily	3710 —

Domain ID domain_id	3u1pA02
Class class	2 — Mainly Beta
Architecture architecture	40 — Beta Barrel
Topology topology	440 — L,D-transpeptidase catalytic domain-like
Homologous superfamily homologous superfamily	10 — L,D-transpeptidase catalytic domain-like

Domain ID domain_id	3u1pB01
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	40 — Immunoglobulin-like
Homologous superfamily homologous superfamily	3710 —

Domain ID domain_id	3u1pB02
Class class	2 — Mainly Beta
Architecture architecture	40 — Beta Barrel
Topology topology	440 — L,D-transpeptidase catalytic domain-like
Homologous superfamily homologous superfamily	10 — L,D-transpeptidase catalytic domain-like

▶

Unit-cell length a length_a	119.044 Å
Unit-cell length b length_b	121.223 Å
Unit-cell length c length_c	122.884 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	16

Space group space_group	I 21 21 21
Space-group number int_tables_number	24
Crystal system crystal_system	—

Resolution resolution	2.800 Å
Low-resolution limit resolution_low	19.840 Å
R factor r_factor	0.1904
R_work r_work	0.1867
R_free r_free	0.2582

Crystal Structure of M. tuberculosis LD-transpeptidase type 2 with Modified Catalytic Cysteine (C354)

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

Mycobacteria Tuberculosis LD-transpeptidase type 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

3u1p__assembly_1__model_1

3u1p__assembly_1__model_1 | I(q)

3u1p__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) 8 domains

SCOP 2.08 (4 domains)

CATH v4.4 (4 domains)

7. Citations (1)

Crystal Structure of M. tuberculosis LD-transpeptidase type 2 with Modified Catalytic Cysteine (C354)

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

Mycobacteria Tuberculosis LD-transpeptidase type 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

3u1p__assembly_1__model_1

3u1p__assembly_1__model_1 | I(q)

3u1p__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) 8 domains

SCOP 2.08 (4 domains)

CATH v4.4 (4 domains)

7. Citations (1)