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2VM1

Crystal structure of barley thioredoxin h isoform 1 crystallized using ammonium sulfate as precipitant

Functional Information from GO Data
ChainGOidnamespacecontents
A0004857molecular_functionenzyme inhibitor activity
A0005737cellular_componentcytoplasm
A0006979biological_processresponse to oxidative stress
A0009409biological_processresponse to cold
A0010497biological_processplasmodesmata-mediated intercellular transport
A0015035molecular_functionprotein-disulfide reductase activity
A0016671molecular_functionoxidoreductase activity, acting on a sulfur group of donors, disulfide as acceptor
B0004857molecular_functionenzyme inhibitor activity
B0005737cellular_componentcytoplasm
B0006979biological_processresponse to oxidative stress
B0009409biological_processresponse to cold
B0010497biological_processplasmodesmata-mediated intercellular transport
B0015035molecular_functionprotein-disulfide reductase activity
B0016671molecular_functionoxidoreductase activity, acting on a sulfur group of donors, disulfide as acceptor
C0004857molecular_functionenzyme inhibitor activity
C0005737cellular_componentcytoplasm
C0006979biological_processresponse to oxidative stress
C0009409biological_processresponse to cold
C0010497biological_processplasmodesmata-mediated intercellular transport
C0015035molecular_functionprotein-disulfide reductase activity
C0016671molecular_functionoxidoreductase activity, acting on a sulfur group of donors, disulfide as acceptor
D0004857molecular_functionenzyme inhibitor activity
D0005737cellular_componentcytoplasm
D0006979biological_processresponse to oxidative stress
D0009409biological_processresponse to cold
D0010497biological_processplasmodesmata-mediated intercellular transport
D0015035molecular_functionprotein-disulfide reductase activity
D0016671molecular_functionoxidoreductase activity, acting on a sulfur group of donors, disulfide as acceptor
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 D1116
ChainResidue
DGLY100
DARG101
DLYS102
DASP103
DHOH2110

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 C1119
ChainResidue
CHOH2110
CGLY100
CARG101
CLYS102
CASP103

site_idAC3
Number of Residues1
DetailsBINDING SITE FOR RESIDUE SO4 D1117
ChainResidue
DLYS108

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 B1116
ChainResidue
BGLY100
BARG101
BLYS102
BASP103
BHOH2133
CPRO48

Functional Information from PROSITE/UniProt
site_idPS00194
Number of Residues19
DetailsTHIOREDOXIN_1 Thioredoxin family active site. IIdFTasWCGPCRvIapvF
ChainResidueDetails
AILE32-PHE50

Catalytic Information from CSA
site_idCSA1
Number of Residues4
DetailsAnnotated By Reference To The Literature 1mek
ChainResidueDetails
APRO42
ACYS40
ACYS43
AGLY41

site_idCSA2
Number of Residues4
DetailsAnnotated By Reference To The Literature 1mek
ChainResidueDetails
BPRO42
BCYS40
BCYS43
BGLY41

site_idCSA3
Number of Residues4
DetailsAnnotated By Reference To The Literature 1mek
ChainResidueDetails
CPRO42
CCYS40
CCYS43
CGLY41

site_idCSA4
Number of Residues4
DetailsAnnotated By Reference To The Literature 1mek
ChainResidueDetails
DPRO42
DCYS40
DCYS43
DGLY41

site_idCSA5
Number of Residues2
DetailsAnnotated By Reference To The Literature 1mek
ChainResidueDetails
ACYS40
ACYS43

site_idCSA6
Number of Residues2
DetailsAnnotated By Reference To The Literature 1mek
ChainResidueDetails
BCYS40
BCYS43

site_idCSA7
Number of Residues2
DetailsAnnotated By Reference To The Literature 1mek
ChainResidueDetails
CCYS40
CCYS43

site_idCSA8
Number of Residues2
DetailsAnnotated By Reference To The Literature 1mek
ChainResidueDetails
DCYS40
DCYS43

223532

PDB entries from 2024-08-07

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