BMRB Entry 4202

Name: Solution Structure of Reduced Monomeric Q133M2 Copper, Zinc Superoxide Dismutase(SOD). Why SOD is a Dimeric Enzyme?
Published: 2000-04-04

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PDB ID: 1ba9
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR4202
MolProbity Validation Chart

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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

Solution Structure of Reduced Monomeric Q133M2 Copper, Zinc Superoxide Dismutase(SOD). Why SOD is a Dimeric Enzyme?

Deposition date:

1997-02-28

Original release date:

2000-04-04

Authors:

Banci, Lucia; Benedetto, Marco; Bertini, Ivano; Del Conte, Rebecca; Piccioli, Mario; Viezzoli, Maria

Citation:

Citation: Banci, Lucia; Benedetto, Marco; Bertini, Ivano; Del Conte, Rebecca; Piccioli, Mario; Viezzoli, Maria. "Solution Structure of Reduced Monomeric Q133M2 Copper, Zinc Superoxide Dismutase (SOD). Why SOD is a Dimeric Enzyme?" Biochemistry 37, 11780-11791 (1998).

Assembly members:

Assembly members:
Superoxide Dismutase, polymer, 153 residues, 16000 Da.
COPPER (II) ION, non-polymer, 63.546 Da.
ZINC ION, non-polymer, 65.409 Da.

Natural source:

Natural source: Common Name: Human Taxonomy ID: 9606 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Homo sapiens

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pBR322

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Superoxide Dismutase: ATKAVAVLKGDGPVQGIINF EQKESNGPVKVWGSIKGLTE GLHGFHVHEEEDNTAGCTSA GPHFNPLSRKHGGPKDEERH VGDLGNVTADKDGVADVSIE DSVISLSGDHSIIGRTLVVH EKADDLGKGGNEQSTKTGNA GSRLACGVIGIAQ

Data sets:

assigned_chemical_shifts
- chemical_shift_assignment_one

Data type	Count
13C chemical shifts	579
15N chemical shifts	157
1H chemical shifts	959

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	Q133M2 SOD	1
2	CU	2
3	Zn	3

Entities:

Entity 1, Q133M2 SOD 153 residues - 16000 Da.

1

ALA

THR

LYS

ALA

VAL

ALA

VAL

LEU

LYS

GLY

2

ASP

GLY

PRO

VAL

GLN

GLY

ILE

ASN

PHE

3

GLU

GLN

LYS

GLU

SER

ASN

GLY

PRO

VAL

LYS

4

VAL

TRP

GLY

SER

ILE

LYS

GLY

LEU

THR

GLU

5

GLY

LEU

HIS

GLY

PHE

HIS

VAL

HIS

GLU

6

GLU

ASP

ASN

THR

ALA

GLY

CYS

THR

SER

ALA

7

GLY

PRO

HIS

PHE

ASN

PRO

LEU

SER

ARG

LYS

8

HIS

GLY

PRO

LYS

ASP

GLU

ARG

HIS

9

VAL

GLY

ASP

LEU

GLY

ASN

VAL

THR

ALA

ASP

10

LYS

ASP

GLY

VAL

ALA

ASP

VAL

SER

ILE

GLU

11

ASP

SER

VAL

ILE

SER

LEU

SER

GLY

ASP

HIS

12

SER

ILE

GLY

ARG

THR

LEU

VAL

HIS

13

GLU

LYS

ALA

ASP

LEU

GLY

LYS

GLY

14

ASN

GLU

GLN

SER

THR

LYS

THR

GLY

ASN

ALA

15

GLY

SER

ARG

LEU

ALA

CYS

GLY

VAL

ILE

GLY

16

ILE

ALA

GLN

Entity 2, CU - Cu - 63.546 Da.

1

CU

Entity 3, Zn - Zn - 65.409 Da.

1

ZN

Samples:

sample_one: Superoxide Dismutase, [U-13C; U-15N], 2 – 3 mM

sample_conditions_one: pH: 5.0 na; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
not available	sample_one	not available	sample_conditions_one

Software:

No software information available

NMR spectrometers:

Bruker AMX 600 MHz
Bruker DRX 600 MHz
Varian Avance 800 MHz
Varian Avance 600 MHz

BMRB	15711 15712 15713 15714 18509 18708 18968 26570
PDB	1BA9 1DSW 1FUN 1KMG 1L3N 1MFM 1N18 1N19 1PTZ 1RK7 1SOS 2AF2 2GBT 2LU5 2XJK 4BCY 4OH2
GB	AAA72747 AAA80237