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4ETM

Crystal structure of YfkJ from Bacillus subtilis

Functional Information from GO Data
ChainGOidnamespacecontents
A0004721molecular_functionphosphoprotein phosphatase activity
A0004725molecular_functionprotein tyrosine phosphatase activity
A0006470biological_processprotein dephosphorylation
A0016787molecular_functionhydrolase activity
B0004721molecular_functionphosphoprotein phosphatase activity
B0004725molecular_functionprotein tyrosine phosphatase activity
B0006470biological_processprotein dephosphorylation
B0016787molecular_functionhydrolase activity
Functional Information from PDB Data
site_idAC1
Number of Residues10
DetailsBINDING SITE FOR RESIDUE PO4 A 201
ChainResidue
ACYS8
BARG-2
ALEU9
AGLY10
AASN11
AILE12
ACYS13
AARG14
AASP125
ATYR127

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE NA A 202
ChainResidue
ALEU79
AASP80
APHE82
AHIS107
AHOH308

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE K A 203
ChainResidue
AASN11
ASER39
ALEU70

site_idAC4
Number of Residues10
DetailsBINDING SITE FOR RESIDUE PO4 B 201
ChainResidue
AARG-2
BCYS8
BLEU9
BGLY10
BASN11
BILE12
BCYS13
BARG14
BASP125
BTYR127

site_idAC5
Number of Residues7
DetailsBINDING SITE FOR RESIDUE NA B 202
ChainResidue
BLEU79
BASP80
BPHE82
BHIS107
BHOH319
BHOH340
BHOH365

site_idAC6
Number of Residues3
DetailsBINDING SITE FOR RESIDUE K B 203
ChainResidue
BASN11
BSER39
BLEU70

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsActive site: {"description":"Nucleophile","evidences":[{"source":"PubMed","id":"15995210","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues2
DetailsActive site: {"evidences":[{"source":"PubMed","id":"15995210","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues2
DetailsActive site: {"description":"Proton donor","evidences":[{"source":"PubMed","id":"15995210","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

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PDB entries from 2025-12-17

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