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4IIR

Crystal Structure of AMPPNP-bound Human PRPF4B kinase domain

Functional Information from GO Data
ChainGOidnamespacecontents
A0004672molecular_functionprotein kinase activity
A0004674molecular_functionprotein serine/threonine kinase activity
A0005524molecular_functionATP binding
A0006468biological_processprotein phosphorylation
A0045292biological_processmRNA cis splicing, via spliceosome
B0004672molecular_functionprotein kinase activity
B0004674molecular_functionprotein serine/threonine kinase activity
B0005524molecular_functionATP binding
B0006468biological_processprotein phosphorylation
B0045292biological_processmRNA cis splicing, via spliceosome
Functional Information from PDB Data
site_idAC1
Number of Residues19
DetailsBINDING SITE FOR RESIDUE ANP A 1101
ChainResidue
ATHR693
AASN773
AASP819
AASN820
ALEU822
AASP834
AMG1103
AHOH1211
AHOH1276
AHOH1327
AHOH1388
ASER699
AVAL701
AALA715
ALYS717
ALEU751
APHE767
AGLU768
ALEU770

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 A 1102
ChainResidue
APTR849
AARG853
AARG856
AHOH1248
AHOH1285
AHOH1305

site_idAC3
Number of Residues2
DetailsBINDING SITE FOR RESIDUE MG A 1103
ChainResidue
AANP1101
AHOH1331

site_idAC4
Number of Residues14
DetailsBINDING SITE FOR RESIDUE ANP B 1101
ChainResidue
BTHR693
BSER699
BVAL701
BALA715
BLYS717
BLEU751
BPHE767
BGLU768
BLEU770
BASN773
BASP819
BASN820
BLEU822
BASP834

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 B 1102
ChainResidue
AARG709
BARG686
BARG709
BHOH1314
BHOH1322
BHOH1377

site_idAC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 B 1103
ChainResidue
BPTR849
BARG853
BARG856
BHOH1228

site_idAC7
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 B 1104
ChainResidue
BLYS804
BARG808
BHOH1258
BHOH1289

Functional Information from PROSITE/UniProt
site_idPS00108
Number of Residues13
DetailsPROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. IlHaDIKpdNILV
ChainResidueDetails
AILE811-VAL823

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":"PRU10027","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues2
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues2
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"18669648","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"20068231","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"21406692","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"Q5RKH1","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

239492

PDB entries from 2025-07-30

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