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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
DetailsACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10028, ECO:0000269|PubMed:19060208
ChainResidueDetails
AASP626
BASP626

site_idSWS_FT_FI2
Number of Residues8
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000269|PubMed:19060208
ChainResidueDetails
AGLU565
AASN571
BLEU487
BLYS517
BGLU565
BASN571
ALEU487
ALYS517

site_idSWS_FT_FI3
Number of Residues4
DetailsMOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:19060208, ECO:0000269|PubMed:19410646
ChainResidueDetails
ATYR466
ATYR588
BTYR466
BTYR588

site_idSWS_FT_FI4
Number of Residues6
DetailsMOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:17803937, ECO:0000269|PubMed:19060208, ECO:0000269|PubMed:19410646
ChainResidueDetails
BTYR656
BTYR657
ATYR586
ATYR656
ATYR657
BTYR586

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PDB entries from 2024-05-01

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