Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

1W89

Structure of the reduced form of human thioredoxin 2

Functional Information from GO Data
ChainGOidnamespacecontents
A0015035molecular_functionprotein-disulfide reductase activity
B0015035molecular_functionprotein-disulfide reductase activity
C0015035molecular_functionprotein-disulfide reductase activity
D0015035molecular_functionprotein-disulfide reductase activity
E0015035molecular_functionprotein-disulfide reductase activity
F0015035molecular_functionprotein-disulfide reductase activity
Functional Information from PROSITE/UniProt
site_idPS00194
Number of Residues19
DetailsTHIOREDOXIN_1 Thioredoxin family active site. VVdFHaqWCGPCKiLgprL
ChainResidueDetails
AVAL23-LEU41

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues630
DetailsDomain: {"description":"Thioredoxin","evidences":[{"source":"PROSITE-ProRule","id":"PRU00691","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues12
DetailsActive site: {"description":"Nucleophile","evidences":[{"source":"UniProtKB","id":"P10599","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues6
DetailsSite: {"description":"Deprotonates C-terminal active site Cys","evidences":[{"source":"UniProtKB","id":"P10599","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues12
DetailsSite: {"description":"Contributes to redox potential value","evidences":[{"source":"UniProtKB","id":"P10599","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues6
DetailsModified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P97493","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues4
DetailsAnnotated By Reference To The Literature 1mek
ChainResidueDetails
ACYS31
ACYS34
APRO33
AGLY32

site_idCSA10
Number of Residues2
DetailsAnnotated By Reference To The Literature 1mek
ChainResidueDetails
DCYS31
DCYS34

site_idCSA11
Number of Residues2
DetailsAnnotated By Reference To The Literature 1mek
ChainResidueDetails
ECYS31
ECYS34

site_idCSA12
Number of Residues2
DetailsAnnotated By Reference To The Literature 1mek
ChainResidueDetails
FCYS31
FCYS34

site_idCSA2
Number of Residues4
DetailsAnnotated By Reference To The Literature 1mek
ChainResidueDetails
BCYS31
BCYS34
BPRO33
BGLY32

site_idCSA3
Number of Residues4
DetailsAnnotated By Reference To The Literature 1mek
ChainResidueDetails
CCYS31
CCYS34
CPRO33
CGLY32

site_idCSA4
Number of Residues4
DetailsAnnotated By Reference To The Literature 1mek
ChainResidueDetails
DCYS31
DCYS34
DPRO33
DGLY32

site_idCSA5
Number of Residues4
DetailsAnnotated By Reference To The Literature 1mek
ChainResidueDetails
ECYS31
ECYS34
EPRO33
EGLY32

site_idCSA6
Number of Residues4
DetailsAnnotated By Reference To The Literature 1mek
ChainResidueDetails
FCYS31
FCYS34
FPRO33
FGLY32

site_idCSA7
Number of Residues2
DetailsAnnotated By Reference To The Literature 1mek
ChainResidueDetails
ACYS31
ACYS34

site_idCSA8
Number of Residues2
DetailsAnnotated By Reference To The Literature 1mek
ChainResidueDetails
BCYS31
BCYS34

site_idCSA9
Number of Residues2
DetailsAnnotated By Reference To The Literature 1mek
ChainResidueDetails
CCYS31
CCYS34

245663

PDB entries from 2025-12-03

PDB statisticsPDBj update infoContact PDBjnumon