1gqq

MURC - Crystal structure of the apo-enzyme from Haemophilus influenzae

Method: X-RAY DIFFRACTION

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

UDP-N-ACETYLMURAMATE-L-ALANINE LIGASE

HAEMOPHILUS INFLUENZAE

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein homooligomer	Homooligomer	Protein 2	No other associated polymer	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	MURC_HAEIN
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–475； UniProt 1–475 Author chain B； PDBConstruct 1–475； UniProt 1–475

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	1gqq
Deposition date deposition_date	2001-12-03
Structure title title	MURC - Crystal structure of the apo-enzyme from Haemophilus influenzae
Keywords keywords	CELL WALL BIOSYNTHESIS, PEPTIDOGLYCAN, MUREIN, LIGASE; CELL WALL BIOSYNTHESIS
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.

1gqq__assembly_1__model_1

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

Download this curve (.dat)

1gqq__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

1gqq__assembly_1__model_1 | P(r) · Pending

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

Rg（Guinier）	36.97 Å
Rg (electron density)	36.83 Å
Total Rg	36.96 Å
Atom count	6578
Residues	855
Excluded volume	117240 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`1gqq__assembly_1__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 (1)

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6. Fold Classification (SCOP + CATH) 12 domains

SCOP 2.08 (6 domains)

Domain ID domain_id	d1gqqa1
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.5 — MurCD N-terminal domain
Superfamily Superfamily superfamily	c.5.1 — MurCD N-terminal domain
Family Family family	c.5.1.1 — MurCD N-terminal domain

Domain ID domain_id	d1gqqa2
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.59 — MurD-like peptide ligases, peptide-binding domain
Superfamily Superfamily superfamily	c.59.1 — MurD-like peptide ligases, peptide-binding domain
Family Family family	c.59.1.1 — MurCDEF C-terminal domain

Domain ID domain_id	d1gqqa3
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.72 — Ribokinase-like
Superfamily Superfamily superfamily	c.72.2 — MurD-like peptide ligases, catalytic domain
Family Family family	c.72.2.1 — MurCDEF

Domain ID domain_id	d1gqqb1
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.5 — MurCD N-terminal domain
Superfamily Superfamily superfamily	c.5.1 — MurCD N-terminal domain
Family Family family	c.5.1.1 — MurCD N-terminal domain

Domain ID domain_id	d1gqqb2
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.59 — MurD-like peptide ligases, peptide-binding domain
Superfamily Superfamily superfamily	c.59.1 — MurD-like peptide ligases, peptide-binding domain
Family Family family	c.59.1.1 — MurCDEF C-terminal domain

Domain ID domain_id	d1gqqb3
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.72 — Ribokinase-like
Superfamily Superfamily superfamily	c.72.2 — MurD-like peptide ligases, catalytic domain
Family Family family	c.72.2.1 — MurCDEF

CATH v4.4 (6 domains)

Domain ID domain_id	1gqqA01
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	50 — Rossmann fold
Homologous superfamily homologous superfamily	720 — NAD(P)-binding Rossmann-like Domain

Domain ID domain_id	1gqqA02
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	1190 — UDP-N-acetylmuramoyl-L-alanine:D-glutamate ligase
Homologous superfamily homologous superfamily	10 — Mur-like, catalytic domain

Domain ID domain_id	1gqqA03
Class class	3 — Alpha Beta
Architecture architecture	90 — Alpha-Beta Complex
Topology topology	190 — Protein-Tyrosine Phosphatase; Chain A
Homologous superfamily homologous superfamily	20 — Mur ligase, C-terminal domain

Domain ID domain_id	1gqqB01
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	50 — Rossmann fold
Homologous superfamily homologous superfamily	720 — NAD(P)-binding Rossmann-like Domain

Domain ID domain_id	1gqqB02
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	1190 — UDP-N-acetylmuramoyl-L-alanine:D-glutamate ligase
Homologous superfamily homologous superfamily	10 — Mur-like, catalytic domain

Domain ID domain_id	1gqqB03
Class class	3 — Alpha Beta
Architecture architecture	90 — Alpha-Beta Complex
Topology topology	190 — Protein-Tyrosine Phosphatase; Chain A
Homologous superfamily homologous superfamily	20 — Mur ligase, C-terminal domain

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Unit-cell length a length_a	65.508 Å
Unit-cell length b length_b	99.485 Å
Unit-cell length c length_c	180.590 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	8

Space group space_group	P 21 21 21
Space-group number int_tables_number	19
Crystal system crystal_system	—

Resolution resolution	3.100 Å
Low-resolution limit resolution_low	19.880 Å
R factor r_factor	0.2413
R_work r_work	0.2389
R_free r_free	0.2862

Description description	UDP-N-ACETYLMURAMATE-L-ALANINE LIGASE
Molecular weight formula_weight	52057.2 kDa
EC 编号 ec_number	6.3.2.8
Source method src_method	man
Copy count entity_count	2

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B
Atom count atom_count	6578

MURC - Crystal structure of the apo-enzyme from Haemophilus influenzae

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

UDP-N-ACETYLMURAMATE-L-ALANINE LIGASE

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

1gqq__assembly_1__model_1

1gqq__assembly_1__model_1 | I(q)

1gqq__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 (1)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

6. Fold Classification (SCOP + CATH) 12 domains

SCOP 2.08 (6 domains)

CATH v4.4 (6 domains)

7. Citations (1)

Source organism organism	HAEMOPHILUS INFLUENZAE
NCBI taxonomy ID ncbi_taxonomy_id	727
Host organism host_organism	Escherichia coli BL21

MURC - Crystal structure of the apo-enzyme from Haemophilus influenzae

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

UDP-N-ACETYLMURAMATE-L-ALANINE LIGASE

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

1gqq__assembly_1__model_1

1gqq__assembly_1__model_1 | I(q)

1gqq__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 (1)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

6. Fold Classification (SCOP + CATH) 12 domains

SCOP 2.08 (6 domains)

CATH v4.4 (6 domains)

7. Citations (1)