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3B2T

Structure of phosphotransferase

Functional Information from GO Data
ChainGOidnamespacecontents
A0004672molecular_functionprotein kinase activity
A0005524molecular_functionATP binding
A0006468biological_processprotein phosphorylation
B0004672molecular_functionprotein kinase activity
B0005524molecular_functionATP binding
B0006468biological_processprotein phosphorylation
Functional Information from PDB Data
site_idAC1
Number of Residues7
DetailsBINDING SITE FOR RESIDUE PO4 B 1
ChainResidue
ALYS526
BTHR661
BGLY663
BARG664
BARG678
BHOH2060
BHOH2218

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE PO4 A 2
ChainResidue
AARG678
AHOH2049
AHOH2106
BLYS526
ATHR661
AGLY663

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE PO4 A 1
ChainResidue
AARG721
AARG737
ATRP740
AHIS741
AHOH2040
AHOH2050

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE PO4 B 2
ChainResidue
BARG721
BARG737
BTRP740
BHIS741
BHOH2053
BHOH2093

site_idAC5
Number of Residues11
DetailsBINDING SITE FOR RESIDUE M33 A 1996
ChainResidue
ALEU487
AGLU489
AGLY490
AALA515
AGLU565
AALA567
ALEU633
AASP644
AHOH2074
AHOH2087
AHOH2256

site_idAC6
Number of Residues11
DetailsBINDING SITE FOR RESIDUE M33 B 1996
ChainResidue
BLEU487
BALA515
BILE548
BGLU565
BALA567
BASN571
BASN631
BLEU633
BASP644
BHOH2069
BHOH2080

Functional Information from PROSITE/UniProt
site_idPS00107
Number of Residues31
DetailsPROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGEGCFGQVVmAeavgidkdkpkeavt...VAVK
ChainResidueDetails
ALEU487-LYS517

site_idPS00109
Number of Residues13
DetailsPROTEIN_KINASE_TYR Tyrosine protein kinases specific active-site signature. CIHrDLTARNVLV
ChainResidueDetails
ACYS622-VAL634

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"},{"source":"PROSITE-ProRule","id":"PRU10028","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"19060208","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues16
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"19060208","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues2
DetailsModified residue: {"description":"Phosphotyrosine; by autocatalysis","evidences":[{"source":"PubMed","id":"19060208","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19410646","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues4
DetailsModified residue: {"description":"Phosphotyrosine; by autocatalysis","evidences":[{"source":"PubMed","id":"17803937","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19060208","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19410646","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
AASP626
AARG630

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
BASP626
BARG630

site_idCSA3
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
AASP626
ATHR628

site_idCSA4
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
BASP626
BTHR628

site_idCSA5
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
ATHR661
AASP626
ATHR628

site_idCSA6
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
BTHR661
BASP626
BTHR628

site_idCSA7
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
AASP626
ATHR628
AASN631

site_idCSA8
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
BASP626
BTHR628
BASN631

246704

PDB entries from 2025-12-24

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