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

4FN6

Structural Characterization of Thiaminase type II TenA from Staphylococcus aureus

Functional Information from GO Data
ChainGOidnamespacecontents
A0005829cellular_componentcytosol
A0006772biological_processthiamine metabolic process
A0009228biological_processthiamine biosynthetic process
A0009229biological_processthiamine diphosphate biosynthetic process
A0016787molecular_functionhydrolase activity
A0050334molecular_functionthiaminase activity
B0005829cellular_componentcytosol
B0006772biological_processthiamine metabolic process
B0009228biological_processthiamine biosynthetic process
B0009229biological_processthiamine diphosphate biosynthetic process
B0016787molecular_functionhydrolase activity
B0050334molecular_functionthiaminase activity
C0005829cellular_componentcytosol
C0006772biological_processthiamine metabolic process
C0009228biological_processthiamine biosynthetic process
C0009229biological_processthiamine diphosphate biosynthetic process
C0016787molecular_functionhydrolase activity
C0050334molecular_functionthiaminase activity
D0005829cellular_componentcytosol
D0006772biological_processthiamine metabolic process
D0009228biological_processthiamine biosynthetic process
D0009229biological_processthiamine diphosphate biosynthetic process
D0016787molecular_functionhydrolase activity
D0050334molecular_functionthiaminase activity
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ACT A 301
ChainResidue
ASER190
AASP191
AHOH431
CSER188
CMET189

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ACT A 302
ChainResidue
AASP44
ATYR47
ACME137
AGLU208

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE GOL A 303
ChainResidue
AASP21
AASP22
AASN213
AHOH423

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ACT B 301
ChainResidue
BLYS6
BGLN9
BALA10
BLYS198

site_idAC5
Number of Residues1
DetailsBINDING SITE FOR RESIDUE ACT B 302
ChainResidue
BASP21

site_idAC6
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL B 303
ChainResidue
BHIS122
BSER123
BGLU125
CLYS61
CALA121
CHIS122
CARG124

site_idAC7
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL C 301
ChainResidue
CASP44
CPHE51
CTYR113
CCME137
CTYR141
CGLU208

site_idAC8
Number of Residues1
DetailsBINDING SITE FOR RESIDUE GOL C 302
ChainResidue
CTRP106

site_idAC9
Number of Residues2
DetailsBINDING SITE FOR RESIDUE ACT C 303
ChainResidue
BSER190
CSER188

site_idBC1
Number of Residues2
DetailsBINDING SITE FOR RESIDUE ACT C 304
ChainResidue
CMET78
CCME137

site_idBC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ACT D 301
ChainResidue
DASP44
DPHE51
DCME137
DTYR141
DGLU208

site_idBC3
Number of Residues1
DetailsBINDING SITE FOR RESIDUE ACT D 302
ChainResidue
DGLU157

site_idBC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE ACT D 303
ChainResidue
AHIS122
ASER123
DSER123

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsActive site: {"description":"Nucleophile","evidences":[{"source":"UniProtKB","id":"P25052","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues4
DetailsActive site: {"description":"Proton donor","evidences":[{"source":"UniProtKB","id":"P25052","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues12
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"P25052","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues4
DetailsSite: {"description":"Increases nucleophilicity of active site Cys","evidences":[{"source":"UniProtKB","id":"P25052","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

249697

PDB entries from 2026-02-25

PDB statisticsPDBj update infoContact PDBjnumon