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5LMA

HUMAN SPLEEN TYROSINE KINASE KINASE DOMAIN IN COMPLEX WITH AZANAPHTHYRIDINE INHIBITOR

Functional Information from GO Data
ChainGOidnamespacecontents
A0004672molecular_functionprotein kinase activity
A0004713molecular_functionprotein tyrosine kinase activity
A0005524molecular_functionATP binding
A0006468biological_processprotein phosphorylation
Functional Information from PDB Data
site_idAC1
Number of Residues14
Detailsbinding site for residue 6ZG A 701
ChainResidue
ALEU377
AASN499
ALEU501
AASP512
AGOL702
AHOH1004
AVAL385
AALA400
AGLU449
AMET450
AALA451
AGLU452
AGLY454
AARG498

site_idAC2
Number of Residues9
Detailsbinding site for residue GOL A 702
ChainResidue
AVAL385
ALYS402
AGLU420
AMET448
ASER511
AASP512
A6ZG701
AHOH829
AHOH835

site_idAC3
Number of Residues7
Detailsbinding site for residue GOL A 703
ChainResidue
AVAL363
AALA421
AASN422
AGLN425
AHOH862
AHOH888
AHOH958

site_idAC4
Number of Residues4
Detailsbinding site for residue DMS A 704
ChainResidue
AASN406
AGLN477
ATYR507
AHOH1057

Functional Information from PROSITE/UniProt
site_idPS00107
Number of Residues26
DetailsPROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGSGNFGTVKkGyyqmkkvvkt........VAVK
ChainResidueDetails
ALEU377-LYS402

site_idPS00109
Number of Residues13
DetailsPROTEIN_KINASE_TYR Tyrosine protein kinases specific active-site signature. FVHrDLAARNVLL
ChainResidueDetails
APHE490-LEU502

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"},{"source":"PROSITE-ProRule","id":"PRU10028","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues9
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues3
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"21469132","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"21469132","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues3
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"21469132","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues1
DetailsModified residue: {"description":"Phosphotyrosine; by autocatalysis","evidences":[{"source":"PubMed","id":"21469132","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues1
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"P48025","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

240971

PDB entries from 2025-08-27

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