2v4i

Structure of a novel N-acyl-enzyme intermediate of an N-terminal nucleophile (Ntn) hydrolase, OAT2

Method: X-RAY DIFFRACTION

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

GLUTAMATE N-ACETYLTRANSFERASE 2 ALPHA CHAIN

STREPTOMYCES CLAVULIGERUS

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein homooligomer	Homooligomer	Protein 4	water × 4	Consistent with protein count
2	Protein homooligomer	Homooligomer	Protein 4	water × 4	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	GNAT2_STRCL
Isoform	—
PDB entities	1, 2
Chains and sequence ranges	Author chain A； PDBConstruct 1–173； UniProt 8–180 Author chain C； PDBConstruct 1–173； UniProt 8–180 Author chain E； PDBConstruct 1–173； UniProt 8–180 Author chain G； PDBConstruct 1–173； UniProt 8–180 Author chain B； PDBConstruct 1–213； UniProt 181–393 Author chain D； PDBConstruct 1–213； UniProt 181–393 Author chain F； PDBConstruct 1–213； UniProt 181–393 Author chain H； PDBConstruct 1–213； UniProt 181–393

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	2v4i
Deposition date deposition_date	2008-09-22
Structure title title	Structure of a novel N-acyl-enzyme intermediate of an N-terminal nucleophile (Ntn) hydrolase, OAT2
Keywords keywords	CYTOPLASM, ACYL ENZYME, TRANSFERASE, NTN HYDROLASE, ACYLTRANSFERASE, ORNITHINE ACETYL TRANSFERASE; TRANSFERASE
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.

2v4i__assembly_1__model_1

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

Download this curve (.dat)

2v4i__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

2v4i__assembly_1__model_1 | P(r) · Pending

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

Rg（Guinier）	28.87 Å
Rg (electron density)	28.28 Å
Total Rg	28.77 Å
Atom count	5426
Residues	750
Excluded volume	95910 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`2v4i__assembly_1__model_1`	tetrameric （4）	Success	4.1.3-1-20251215 (887e7ef)	View Download
2	1	`2v4i__assembly_2__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 (3)

Entity 1 Entity 1 polymer

Description description	GLUTAMATE N-ACETYLTRANSFERASE 2 ALPHA CHAIN
Molecular weight formula_weight	18089.5 kDa
EC 编号 ec_number	2.3.1.35
Source method src_method	man
Copy count entity_count	4

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,C,E,G
Atom count atom_count	11153

TPRGFVVHTAPVGLADDGRDDFTVLASTAPATVSAVFTRSRFAGPSVVLCREAVADGQARGVVVLARNANVATGLEGEENAREVREAVARALGLPEGEMLIASTGVIGRQYPMESIREHLKTLEWPAGEGGFDRAARAIMTTDTRPKEVRVSVGGATLVGIAKGVGMLEPDMA

Source Source

Source organism organism	STREPTOMYCES CLAVULIGERUS
NCBI taxonomy ID ncbi_taxonomy_id	1901
Host organism host_organism	ESCHERICHIA COLI

Entity 2 Entity 2 polymer

Description description	GLUTAMATE N-ACETYLTRANSFERASE 2 BETA CHAIN
Molecular weight formula_weight	22846.3 kDa
EC 编号 ec_number	2.3.1.35
Mutation mutation	YES
Source method src_method	man
Copy count entity_count	4

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	B,D,F,H

ALLTFFATDARLDPAEQDRLFRRVMDRTFNAVSIDTDTSTSDTAVLFANGLAGEVDAGEFEEALHTAALALVKDIASDGEGAAKLIEVQVTGARDDAQAKRVGKTVVNSPLVKTAVHGCDPNWGRVAMAIGKCSDDTDIDQERVTIRFGEVEVYPPKARGDQADDALRAAVAEHLRGDEVVIGIDLAIADGAFTVYGCDLTEGYVRLNSEYTT

Source Source

Source organism organism	STREPTOMYCES CLAVULIGERUS
NCBI taxonomy ID ncbi_taxonomy_id	1901
Host organism host_organism	ESCHERICHIA COLI

Entity 3 Entity 3 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	301

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6. Fold Classification (SCOP + CATH) 12 domains

CATH v4.4 (12 domains)

Domain ID domain_id	2v4iA00
Class class	3 — Alpha Beta
Architecture architecture	60 — 4-Layer Sandwich
Topology topology	70 — L-amino peptidase D-ALA esterase/amidase
Homologous superfamily homologous superfamily	12 — L-amino peptidase D-ALA esterase/amidase

Domain ID domain_id	2v4iB01
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	2330 — arginine biosynthesis bifunctional protein fold
Homologous superfamily homologous superfamily	10 — arginine biosynthesis bifunctional protein suprefamily

Domain ID domain_id	2v4iB02
Class class	3 — Alpha Beta
Architecture architecture	10 — Roll
Topology topology	20 — Ubiquitin-like (UB roll)
Homologous superfamily homologous superfamily	340 — ArgJ beta chain, C-terminal domain

Domain ID domain_id	2v4iC00
Class class	3 — Alpha Beta
Architecture architecture	60 — 4-Layer Sandwich
Topology topology	70 — L-amino peptidase D-ALA esterase/amidase
Homologous superfamily homologous superfamily	12 — L-amino peptidase D-ALA esterase/amidase

Domain ID domain_id	2v4iD01
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	2330 — arginine biosynthesis bifunctional protein fold
Homologous superfamily homologous superfamily	10 — arginine biosynthesis bifunctional protein suprefamily

Domain ID domain_id	2v4iD02
Class class	3 — Alpha Beta
Architecture architecture	10 — Roll
Topology topology	20 — Ubiquitin-like (UB roll)
Homologous superfamily homologous superfamily	340 — ArgJ beta chain, C-terminal domain

Domain ID domain_id	2v4iE00
Class class	3 — Alpha Beta
Architecture architecture	60 — 4-Layer Sandwich
Topology topology	70 — L-amino peptidase D-ALA esterase/amidase
Homologous superfamily homologous superfamily	12 — L-amino peptidase D-ALA esterase/amidase

Domain ID domain_id	2v4iF01
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	2330 — arginine biosynthesis bifunctional protein fold
Homologous superfamily homologous superfamily	10 — arginine biosynthesis bifunctional protein suprefamily

Domain ID domain_id	2v4iF02
Class class	3 — Alpha Beta
Architecture architecture	10 — Roll
Topology topology	20 — Ubiquitin-like (UB roll)
Homologous superfamily homologous superfamily	340 — ArgJ beta chain, C-terminal domain

Domain ID domain_id	2v4iG00
Class class	3 — Alpha Beta
Architecture architecture	60 — 4-Layer Sandwich
Topology topology	70 — L-amino peptidase D-ALA esterase/amidase
Homologous superfamily homologous superfamily	12 — L-amino peptidase D-ALA esterase/amidase

Domain ID domain_id	2v4iH01
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	2330 — arginine biosynthesis bifunctional protein fold
Homologous superfamily homologous superfamily	10 — arginine biosynthesis bifunctional protein suprefamily

Domain ID domain_id	2v4iH02
Class class	3 — Alpha Beta
Architecture architecture	10 — Roll
Topology topology	20 — Ubiquitin-like (UB roll)
Homologous superfamily homologous superfamily	340 — ArgJ beta chain, C-terminal domain

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Unit-cell length a length_a	73.455 Å
Unit-cell length b length_b	180.163 Å
Unit-cell length c length_c	60.962 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 1 21 1
Space-group number int_tables_number	4
Crystal system crystal_system	—

Resolution resolution	2.200 Å
Low-resolution limit resolution_low	29.700 Å
R factor r_factor	0.2156
R_work r_work	0.2140
R_free r_free	0.2466

Structure of a novel N-acyl-enzyme intermediate of an N-terminal nucleophile (Ntn) hydrolase, OAT2

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

GLUTAMATE N-ACETYLTRANSFERASE 2 ALPHA CHAIN

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

2v4i__assembly_1__model_1

2v4i__assembly_1__model_1 | I(q)

2v4i__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 polymer

Polymer Polymer

Source Source

Entity 3 Entity 3 water

6. Fold Classification (SCOP + CATH) 12 domains

CATH v4.4 (12 domains)

7. Citations (2)

Structure of a novel N-acyl-enzyme intermediate of an N-terminal nucleophile (Ntn) hydrolase, OAT2

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

GLUTAMATE N-ACETYLTRANSFERASE 2 ALPHA CHAIN

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

2v4i__assembly_1__model_1

2v4i__assembly_1__model_1 | I(q)

2v4i__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 polymer

Polymer Polymer

Source Source

Entity 3 Entity 3 water

6. Fold Classification (SCOP + CATH) 12 domains

CATH v4.4 (12 domains)

7. Citations (2)