2vut

Crystal structure of NAD-bound NmrA-AreA zinc finger complex

Method: X-RAY DIFFRACTION

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

NITROGEN METABOLITE REPRESSION REGULATOR NMRA

Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139)

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 2	NITROGEN REGULATORY PROTEIN AREA × 1 （P17429） NICOTINAMIDE-ADENINE-DINUCLEOTIDE × 1 CHLORIDE ION × 1 ZINC ION × 1 water × 2	Consistent with protein count
10	Protein monomer	Monomer	Protein 1	NICOTINAMIDE-ADENINE-DINUCLEOTIDE × 1 water × 1	Consistent with protein count
11	Protein monomer	Monomer	Protein 1	NICOTINAMIDE-ADENINE-DINUCLEOTIDE × 1 CHLORIDE ION × 1 GLYCEROL × 1 water × 1	Consistent with protein count
12	Protein monomer	Monomer	Protein 1	NICOTINAMIDE-ADENINE-DINUCLEOTIDE × 1 CHLORIDE ION × 1 water × 1	Consistent with protein count
13	Protein monomer	Monomer	Protein 1	NICOTINAMIDE-ADENINE-DINUCLEOTIDE × 1 CHLORIDE ION × 1 water × 1	Consistent with protein count
14	Protein monomer	Monomer	Protein 1	NICOTINAMIDE-ADENINE-DINUCLEOTIDE × 1 CHLORIDE ION × 1 water × 1	Consistent with protein count
15	Protein monomer	Monomer	Protein 1	NICOTINAMIDE-ADENINE-DINUCLEOTIDE × 1 CHLORIDE ION × 1 GLYCEROL × 1 water × 1	Consistent with protein count
16	Protein monomer	Monomer	Protein 1	NICOTINAMIDE-ADENINE-DINUCLEOTIDE × 1 CHLORIDE ION × 1 water × 1	Consistent with protein count
2	Protein heterocomplex	Heteromer	Protein 2	NITROGEN REGULATORY PROTEIN AREA × 1 （P17429） NICOTINAMIDE-ADENINE-DINUCLEOTIDE × 1 ZINC ION × 1 water × 2	Consistent with protein count
3	Protein heterocomplex	Heteromer	Protein 2	NITROGEN REGULATORY PROTEIN AREA × 1 （P17429） NICOTINAMIDE-ADENINE-DINUCLEOTIDE × 1 CHLORIDE ION × 1 GLYCEROL × 1 ZINC ION × 1 water × 2	Consistent with protein count
4	Protein heterocomplex	Heteromer	Protein 2	NITROGEN REGULATORY PROTEIN AREA × 1 （P17429） NICOTINAMIDE-ADENINE-DINUCLEOTIDE × 1 CHLORIDE ION × 1 ZINC ION × 1 water × 2	Consistent with protein count
5	Protein heterocomplex	Heteromer	Protein 2	NITROGEN REGULATORY PROTEIN AREA × 1 （P17429） NICOTINAMIDE-ADENINE-DINUCLEOTIDE × 1 CHLORIDE ION × 1 GLYCEROL × 1 ZINC ION × 1 water × 2	Consistent with protein count
6	Protein heterocomplex	Heteromer	Protein 2	NITROGEN REGULATORY PROTEIN AREA × 1 （P17429） NICOTINAMIDE-ADENINE-DINUCLEOTIDE × 1 CHLORIDE ION × 1 ZINC ION × 1 water × 2	Consistent with protein count
7	Protein heterocomplex	Heteromer	Protein 2	NITROGEN REGULATORY PROTEIN AREA × 1 （P17429） NICOTINAMIDE-ADENINE-DINUCLEOTIDE × 1 CHLORIDE ION × 1 GLYCEROL × 1 ZINC ION × 1 water × 2	Consistent with protein count
8	Protein heterocomplex	Heteromer	Protein 2	NITROGEN REGULATORY PROTEIN AREA × 1 （P17429） NICOTINAMIDE-ADENINE-DINUCLEOTIDE × 1 CHLORIDE ION × 1 ZINC ION × 1 water × 2	Consistent with protein count
9	Protein monomer	Monomer	Protein 1	NICOTINAMIDE-ADENINE-DINUCLEOTIDE × 1 CHLORIDE ION × 1 water × 1	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	O59919_EMENI
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–352； UniProt 1–352 Author chain B； PDBConstruct 1–352； UniProt 1–352 Author chain C； PDBConstruct 1–352； UniProt 1–352 Author chain D； PDBConstruct 1–352； UniProt 1–352 Author chain E； PDBConstruct 1–352； UniProt 1–352 Author chain F； PDBConstruct 1–352； UniProt 1–352 Author chain G； PDBConstruct 1–352； UniProt 1–352 Author chain H； PDBConstruct 1–352； UniProt 1–352

NITROGEN REGULATORY PROTEIN AREA

EMERICELLA NIDULANS

UniProt P17429

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 2	NITROGEN METABOLITE REPRESSION REGULATOR NMRA × 1 （O59919） NICOTINAMIDE-ADENINE-DINUCLEOTIDE × 1 CHLORIDE ION × 1 ZINC ION × 1 water × 2	Consistent with protein count
17	Protein monomer	Monomer	Protein 1	ZINC ION × 1 water × 1	Consistent with protein count
18	Protein monomer	Monomer	Protein 1	ZINC ION × 1 water × 1	Consistent with protein count
19	Protein monomer	Monomer	Protein 1	ZINC ION × 1 water × 1	Consistent with protein count
2	Protein heterocomplex	Heteromer	Protein 2	NITROGEN METABOLITE REPRESSION REGULATOR NMRA × 1 （O59919） NICOTINAMIDE-ADENINE-DINUCLEOTIDE × 1 ZINC ION × 1 water × 2	Consistent with protein count
20	Protein monomer	Monomer	Protein 1	ZINC ION × 1 water × 1	Consistent with protein count
21	Protein monomer	Monomer	Protein 1	GLYCEROL × 1 ZINC ION × 1 water × 1	Consistent with protein count
22	Protein monomer	Monomer	Protein 1	ZINC ION × 1 water × 1	Consistent with protein count
23	Protein monomer	Monomer	Protein 1	ZINC ION × 1 water × 1	Consistent with protein count
24	Protein monomer	Monomer	Protein 1	ZINC ION × 1 water × 1	Consistent with protein count
3	Protein heterocomplex	Heteromer	Protein 2	NITROGEN METABOLITE REPRESSION REGULATOR NMRA × 1 （O59919） NICOTINAMIDE-ADENINE-DINUCLEOTIDE × 1 CHLORIDE ION × 1 GLYCEROL × 1 ZINC ION × 1 water × 2	Consistent with protein count
4	Protein heterocomplex	Heteromer	Protein 2	NITROGEN METABOLITE REPRESSION REGULATOR NMRA × 1 （O59919） NICOTINAMIDE-ADENINE-DINUCLEOTIDE × 1 CHLORIDE ION × 1 ZINC ION × 1 water × 2	Consistent with protein count
5	Protein heterocomplex	Heteromer	Protein 2	NITROGEN METABOLITE REPRESSION REGULATOR NMRA × 1 （O59919） NICOTINAMIDE-ADENINE-DINUCLEOTIDE × 1 CHLORIDE ION × 1 GLYCEROL × 1 ZINC ION × 1 water × 2	Consistent with protein count
6	Protein heterocomplex	Heteromer	Protein 2	NITROGEN METABOLITE REPRESSION REGULATOR NMRA × 1 （O59919） NICOTINAMIDE-ADENINE-DINUCLEOTIDE × 1 CHLORIDE ION × 1 ZINC ION × 1 water × 2	Consistent with protein count
7	Protein heterocomplex	Heteromer	Protein 2	NITROGEN METABOLITE REPRESSION REGULATOR NMRA × 1 （O59919） NICOTINAMIDE-ADENINE-DINUCLEOTIDE × 1 CHLORIDE ION × 1 GLYCEROL × 1 ZINC ION × 1 water × 2	Consistent with protein count
8	Protein heterocomplex	Heteromer	Protein 2	NITROGEN METABOLITE REPRESSION REGULATOR NMRA × 1 （O59919） NICOTINAMIDE-ADENINE-DINUCLEOTIDE × 1 CHLORIDE ION × 1 ZINC ION × 1 water × 2	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	AREA_EMENI
Isoform	—
PDB entities	2
Chains and sequence ranges	Author chain I； PDBConstruct 1–43； UniProt 670–712 Author chain J； PDBConstruct 1–43； UniProt 670–712 Author chain K； PDBConstruct 1–43； UniProt 670–712 Author chain L； PDBConstruct 1–43； UniProt 670–712 Author chain M； PDBConstruct 1–43； UniProt 670–712 Author chain N； PDBConstruct 1–43； UniProt 670–712 Author chain O； PDBConstruct 1–43； UniProt 670–712 Author chain P； PDBConstruct 1–43； UniProt 670–712

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	2vut
Deposition date deposition_date	2008-05-30
Structure title title	Crystal structure of NAD-bound NmrA-AreA zinc finger complex
Keywords keywords	;TRANSCRIPTION REGULATION, PROTEIN-PROTEIN INTERACTIONS, METAL-BINDING, NITRATE ASSIMILATION, ZINC-FINGER, DNA-BINDING, ZINC FINGERS, TRANSCRIPTION, ZINC, AREA, NMRA, NUCLEUS, ACTIVATOR, GATA-TYPE ;; TRANSCRIPTION
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.

2vut__assembly_20__model_1

Assembly 20 · Model 1 · CRYSOL 4.1.3-1-20251215 (887e7ef)

Download this curve (.dat)

2vut__assembly_20__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

2vut__assembly_20__model_1 | P(r) · Pending

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

Rg（Guinier）	10.67 Å
Rg (electron density)	9.64 Å
Total Rg	11.03 Å
Atom count	327
Residues	42
Excluded volume	5874 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`2vut__assembly_1__model_1`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
2	1	`2vut__assembly_2__model_1`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
3	1	`2vut__assembly_3__model_1`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
4	1	`2vut__assembly_4__model_1`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
5	1	`2vut__assembly_5__model_1`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
6	1	`2vut__assembly_6__model_1`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
7	1	`2vut__assembly_7__model_1`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
8	1	`2vut__assembly_8__model_1`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
9	1	`2vut__assembly_9__model_1`	monomeric （1）	Success	4.1.3-1-20251215 (887e7ef)	View Download
10	1	`2vut__assembly_10__model_1`	monomeric （1）	Success	4.1.3-1-20251215 (887e7ef)	View Download
11	1	`2vut__assembly_11__model_1`	monomeric （1）	Success	4.1.3-1-20251215 (887e7ef)	View Download
12	1	`2vut__assembly_12__model_1`	monomeric （1）	Success	4.1.3-1-20251215 (887e7ef)	View Download
13	1	`2vut__assembly_13__model_1`	monomeric （1）	Success	4.1.3-1-20251215 (887e7ef)	View Download
14	1	`2vut__assembly_14__model_1`	monomeric （1）	Success	4.1.3-1-20251215 (887e7ef)	View Download
15	1	`2vut__assembly_15__model_1`	monomeric （1）	Success	4.1.3-1-20251215 (887e7ef)	View Download
16	1	`2vut__assembly_16__model_1`	monomeric （1）	Success	4.1.3-1-20251215 (887e7ef)	View Download
17	1	`2vut__assembly_17__model_1`	monomeric （1）	Success	4.1.3-1-20251215 (887e7ef)	View Download
18	1	`2vut__assembly_18__model_1`	monomeric （1）	Success	4.1.3-1-20251215 (887e7ef)	View Download
19	1	`2vut__assembly_19__model_1`	monomeric （1）	Success	4.1.3-1-20251215 (887e7ef)	View Download
20	1	`2vut__assembly_20__model_1`	monomeric （1）	Success	4.1.3-1-20251215 (887e7ef)	View Download
21	1	`2vut__assembly_21__model_1`	monomeric （1）	Success	4.1.3-1-20251215 (887e7ef)	View Download
22	1	`2vut__assembly_22__model_1`	monomeric （1）	Success	4.1.3-1-20251215 (887e7ef)	View Download
23	1	`2vut__assembly_23__model_1`	monomeric （1）	Success	4.1.3-1-20251215 (887e7ef)	View Download
24	1	`2vut__assembly_24__model_1`	monomeric （1）	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 (7)

Entity 1 Entity 1 polymer

Description description	NITROGEN METABOLITE REPRESSION REGULATOR NMRA
Molecular weight formula_weight	38835.2 kDa
Source method src_method	man
Copy count entity_count	8

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B,C,D,E,F,G,H
Atom count atom_count	25234

MAQQKKTIAVVNATGRQAASLIRVAAAVGHHVRAQVHSLKGLIAEELQAIPNVTLFQGPLLNNVPLMDTLFEGAHLAFINTTSQAGDEIAIGKDLADAAKRAGTIQHYIYSSMPDHSLYGPWPAVPMWAPKFTVENYVRQLGLPSTFVYAGIYNNNFTSLPYPLFQMELMPDGTFEWHAPFDPDIPLPWLDAEHDVGPALLQIFKDGPQKWNGHRIALTFETLSPVQVCAAFSRALNRRVTYVQVPKVEIKVNIPVGYREQLEAIEVVFGEHKAPYFPLPEFSRPAAGSPKGLGPANGKGAGAGMMQGPGGVISQRVTDEARKLWSGWRDMEEYAREVFPIEEEANGLDWML

Source Source

Source organism organism	Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139)
Common name common_name	Aspergillus nidulans
NCBI taxonomy ID ncbi_taxonomy_id	227321
Host organism host_organism	ESCHERICHIA COLI

Entity 2 Entity 2 polymer

Description description	NITROGEN REGULATORY PROTEIN AREA
Molecular weight formula_weight	4789.6 kDa
Source method src_method	man
Copy count entity_count	8

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	I,J,K,L,M,N,O,P

PTTCTNCFTQTTPLWRRNPEGQPLCNACGLFLKLHGVVRPLSL

Source Source

Source organism organism	EMERICELLA NIDULANS
Common name common_name	Aspergillus nidulans
NCBI taxonomy ID ncbi_taxonomy_id	227321
Host organism host_organism	ESCHERICHIA COLI

Entity 3 Entity 3 non-polymer

Description description	NICOTINAMIDE-ADENINE-DINUCLEOTIDE
Molecular weight formula_weight	663.4 kDa
Source method src_method	syn
Copy count entity_count	8

Entity 4 Entity 4 non-polymer

Description description	CHLORIDE ION
Molecular weight formula_weight	35.5 kDa
Source method src_method	syn
Copy count entity_count	7

Entity 5 Entity 5 non-polymer

Description description	GLYCEROL
Molecular weight formula_weight	92.1 kDa
Source method src_method	syn
Copy count entity_count	3

Entity 6 Entity 6 non-polymer

Description description	ZINC ION
Molecular weight formula_weight	65.4 kDa
Source method src_method	syn
Copy count entity_count	8

Entity 7 Entity 7 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	1957

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6. Fold Classification (SCOP + CATH) 40 domains

SCOP 2.08 (16 domains)

Domain ID domain_id	d2vuta_
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.2 — NAD(P)-binding Rossmann-fold domains
Superfamily Superfamily superfamily	c.2.1 — NAD(P)-binding Rossmann-fold domains
Family Family family	c.2.1.2 — Tyrosine-dependent oxidoreductases

Domain ID domain_id	d2vutb_
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.2 — NAD(P)-binding Rossmann-fold domains
Superfamily Superfamily superfamily	c.2.1 — NAD(P)-binding Rossmann-fold domains
Family Family family	c.2.1.2 — Tyrosine-dependent oxidoreductases

Domain ID domain_id	d2vutc_
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.2 — NAD(P)-binding Rossmann-fold domains
Superfamily Superfamily superfamily	c.2.1 — NAD(P)-binding Rossmann-fold domains
Family Family family	c.2.1.2 — Tyrosine-dependent oxidoreductases

Domain ID domain_id	d2vutd_
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.2 — NAD(P)-binding Rossmann-fold domains
Superfamily Superfamily superfamily	c.2.1 — NAD(P)-binding Rossmann-fold domains
Family Family family	c.2.1.2 — Tyrosine-dependent oxidoreductases

Domain ID domain_id	d2vute_
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.2 — NAD(P)-binding Rossmann-fold domains
Superfamily Superfamily superfamily	c.2.1 — NAD(P)-binding Rossmann-fold domains
Family Family family	c.2.1.2 — Tyrosine-dependent oxidoreductases

Domain ID domain_id	d2vutf_
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.2 — NAD(P)-binding Rossmann-fold domains
Superfamily Superfamily superfamily	c.2.1 — NAD(P)-binding Rossmann-fold domains
Family Family family	c.2.1.2 — Tyrosine-dependent oxidoreductases

Domain ID domain_id	d2vutg_
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.2 — NAD(P)-binding Rossmann-fold domains
Superfamily Superfamily superfamily	c.2.1 — NAD(P)-binding Rossmann-fold domains
Family Family family	c.2.1.2 — Tyrosine-dependent oxidoreductases

Domain ID domain_id	d2vuth_
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.2 — NAD(P)-binding Rossmann-fold domains
Superfamily Superfamily superfamily	c.2.1 — NAD(P)-binding Rossmann-fold domains
Family Family family	c.2.1.2 — Tyrosine-dependent oxidoreductases

Domain ID domain_id	d2vuti_
Class class	g — Small proteins
Fold Fold fold	g.39 — Glucocorticoid receptor-like (DNA-binding domain)
Superfamily Superfamily superfamily	g.39.1 — Glucocorticoid receptor-like (DNA-binding domain)
Family Family family	g.39.1.0 — automated matches

Domain ID domain_id	d2vutj_
Class class	g — Small proteins
Fold Fold fold	g.39 — Glucocorticoid receptor-like (DNA-binding domain)
Superfamily Superfamily superfamily	g.39.1 — Glucocorticoid receptor-like (DNA-binding domain)
Family Family family	g.39.1.0 — automated matches

Domain ID domain_id	d2vutk_
Class class	g — Small proteins
Fold Fold fold	g.39 — Glucocorticoid receptor-like (DNA-binding domain)
Superfamily Superfamily superfamily	g.39.1 — Glucocorticoid receptor-like (DNA-binding domain)
Family Family family	g.39.1.0 — automated matches

Domain ID domain_id	d2vutl_
Class class	g — Small proteins
Fold Fold fold	g.39 — Glucocorticoid receptor-like (DNA-binding domain)
Superfamily Superfamily superfamily	g.39.1 — Glucocorticoid receptor-like (DNA-binding domain)
Family Family family	g.39.1.0 — automated matches

Domain ID domain_id	d2vutm_
Class class	g — Small proteins
Fold Fold fold	g.39 — Glucocorticoid receptor-like (DNA-binding domain)
Superfamily Superfamily superfamily	g.39.1 — Glucocorticoid receptor-like (DNA-binding domain)
Family Family family	g.39.1.0 — automated matches

Domain ID domain_id	d2vutn_
Class class	g — Small proteins
Fold Fold fold	g.39 — Glucocorticoid receptor-like (DNA-binding domain)
Superfamily Superfamily superfamily	g.39.1 — Glucocorticoid receptor-like (DNA-binding domain)
Family Family family	g.39.1.0 — automated matches

Domain ID domain_id	d2vuto_
Class class	g — Small proteins
Fold Fold fold	g.39 — Glucocorticoid receptor-like (DNA-binding domain)
Superfamily Superfamily superfamily	g.39.1 — Glucocorticoid receptor-like (DNA-binding domain)
Family Family family	g.39.1.0 — automated matches

Domain ID domain_id	d2vutp_
Class class	g — Small proteins
Fold Fold fold	g.39 — Glucocorticoid receptor-like (DNA-binding domain)
Superfamily Superfamily superfamily	g.39.1 — Glucocorticoid receptor-like (DNA-binding domain)
Family Family family	g.39.1.0 — automated matches

CATH v4.4 (24 domains)

Domain ID domain_id	2vutA01
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	2vutA02
Class class	3 — Alpha Beta
Architecture architecture	90 — Alpha-Beta Complex
Topology topology	25 — UDP-galactose 4-epimerase; domain 1
Homologous superfamily homologous superfamily	10 — UDP-galactose 4-epimerase, domain 1

Domain ID domain_id	2vutB01
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	2vutB02
Class class	3 — Alpha Beta
Architecture architecture	90 — Alpha-Beta Complex
Topology topology	25 — UDP-galactose 4-epimerase; domain 1
Homologous superfamily homologous superfamily	10 — UDP-galactose 4-epimerase, domain 1

Domain ID domain_id	2vutC01
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	2vutC02
Class class	3 — Alpha Beta
Architecture architecture	90 — Alpha-Beta Complex
Topology topology	25 — UDP-galactose 4-epimerase; domain 1
Homologous superfamily homologous superfamily	10 — UDP-galactose 4-epimerase, domain 1

Domain ID domain_id	2vutD01
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	2vutD02
Class class	3 — Alpha Beta
Architecture architecture	90 — Alpha-Beta Complex
Topology topology	25 — UDP-galactose 4-epimerase; domain 1
Homologous superfamily homologous superfamily	10 — UDP-galactose 4-epimerase, domain 1

Domain ID domain_id	2vutE01
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	2vutE02
Class class	3 — Alpha Beta
Architecture architecture	90 — Alpha-Beta Complex
Topology topology	25 — UDP-galactose 4-epimerase; domain 1
Homologous superfamily homologous superfamily	10 — UDP-galactose 4-epimerase, domain 1

Domain ID domain_id	2vutF01
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	2vutF02
Class class	3 — Alpha Beta
Architecture architecture	90 — Alpha-Beta Complex
Topology topology	25 — UDP-galactose 4-epimerase; domain 1
Homologous superfamily homologous superfamily	10 — UDP-galactose 4-epimerase, domain 1

Domain ID domain_id	2vutG01
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	2vutG02
Class class	3 — Alpha Beta
Architecture architecture	90 — Alpha-Beta Complex
Topology topology	25 — UDP-galactose 4-epimerase; domain 1
Homologous superfamily homologous superfamily	10 — UDP-galactose 4-epimerase, domain 1

Domain ID domain_id	2vutH01
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	2vutH02
Class class	3 — Alpha Beta
Architecture architecture	90 — Alpha-Beta Complex
Topology topology	25 — UDP-galactose 4-epimerase; domain 1
Homologous superfamily homologous superfamily	10 — UDP-galactose 4-epimerase, domain 1

Domain ID domain_id	2vutI00
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	50 — Erythroid Transcription Factor GATA-1; Chain A
Homologous superfamily homologous superfamily	10 — Erythroid Transcription Factor GATA-1, subunit A

Domain ID domain_id	2vutJ00
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	50 — Erythroid Transcription Factor GATA-1; Chain A
Homologous superfamily homologous superfamily	10 — Erythroid Transcription Factor GATA-1, subunit A

Domain ID domain_id	2vutK00
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	50 — Erythroid Transcription Factor GATA-1; Chain A
Homologous superfamily homologous superfamily	10 — Erythroid Transcription Factor GATA-1, subunit A

Domain ID domain_id	2vutL00
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	50 — Erythroid Transcription Factor GATA-1; Chain A
Homologous superfamily homologous superfamily	10 — Erythroid Transcription Factor GATA-1, subunit A

Domain ID domain_id	2vutM00
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	50 — Erythroid Transcription Factor GATA-1; Chain A
Homologous superfamily homologous superfamily	10 — Erythroid Transcription Factor GATA-1, subunit A

Domain ID domain_id	2vutN00
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	50 — Erythroid Transcription Factor GATA-1; Chain A
Homologous superfamily homologous superfamily	10 — Erythroid Transcription Factor GATA-1, subunit A

Domain ID domain_id	2vutO00
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	50 — Erythroid Transcription Factor GATA-1; Chain A
Homologous superfamily homologous superfamily	10 — Erythroid Transcription Factor GATA-1, subunit A

Domain ID domain_id	2vutP00
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	50 — Erythroid Transcription Factor GATA-1; Chain A
Homologous superfamily homologous superfamily	10 — Erythroid Transcription Factor GATA-1, subunit A

▶

Unit-cell length a length_a	227.520 Å
Unit-cell length b length_b	227.520 Å
Unit-cell length c length_c	222.570 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	90.00 °
Unit-cell angle γ angle_gamma	120.00 °
Molecules per unit cell Z z_pdb	72

Space group space_group	H 3
Space-group number int_tables_number	146
Crystal system crystal_system	—

Resolution resolution	2.300 Å
Low-resolution limit resolution_low	29.860 Å
R factor r_factor	0.2150
R_work r_work	0.2150
R_free r_free	0.2740

Crystal structure of NAD-bound NmrA-AreA zinc finger complex

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

NITROGEN METABOLITE REPRESSION REGULATOR NMRA

State in the Current Structure

Other States of the Same Protein in the Database

NITROGEN REGULATORY PROTEIN AREA

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

2vut__assembly_20__model_1

2vut__assembly_20__model_1 | I(q)

2vut__assembly_20__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 (7)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

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 non-polymer

Entity 6 Entity 6 non-polymer

Entity 7 Entity 7 water

6. Fold Classification (SCOP + CATH) 40 domains

SCOP 2.08 (16 domains)

CATH v4.4 (24 domains)

7. Citations (1)

Crystal structure of NAD-bound NmrA-AreA zinc finger complex

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

NITROGEN METABOLITE REPRESSION REGULATOR NMRA

State in the Current Structure

Other States of the Same Protein in the Database

Monomer

Homodimer

Homotetramer

Other homooligomers

Heteromeric or nucleic-acid complex

NITROGEN REGULATORY PROTEIN AREA

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

2vut__assembly_20__model_1

2vut__assembly_20__model_1 | I(q)

2vut__assembly_20__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 (7)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

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 non-polymer

Entity 6 Entity 6 non-polymer

Entity 7 Entity 7 water

6. Fold Classification (SCOP + CATH) 40 domains

SCOP 2.08 (16 domains)

CATH v4.4 (24 domains)

7. Citations (1)