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4BIE

Crystal Structures of Ask1-inhibitor Complexes

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 Residues5
DetailsBINDING SITE FOR RESIDUE GOL A 1941
ChainResidue
AGLU676
AARG698
AGLN703
AARG705
ATRP770

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL B 1942
ChainResidue
BLYS769
BTRP770
BTHR813
BGLU676
BARG698
BGLN703
BARG705

site_idAC3
Number of Residues11
DetailsBINDING SITE FOR RESIDUE IE6 A 1942
ChainResidue
AGLY687
ALYS688
AGLY689
AVAL694
AALA707
ALYS709
AGLU755
AVAL757
AASN808
ALEU810
AASP822

site_idAC4
Number of Residues18
DetailsBINDING SITE FOR RESIDUE IE6 B 1943
ChainResidue
BLEU686
BGLY687
BLYS688
BGLY689
BVAL694
BALA707
BLYS709
BGLU755
BGLN756
BVAL757
BASP807
BASN808
BLEU810
BASP822
BHOH2013
BHOH2020
BHOH2033
BHOH2036

Functional Information from PROSITE/UniProt
site_idPS00107
Number of Residues24
DetailsPROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGKGTYGIVYaGrdlsnqvr..........IAIK
ChainResidueDetails
ALEU686-LYS709

site_idPS00108
Number of Residues13
DetailsPROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. IvHrDIKgdNVLI
ChainResidueDetails
AILE799-ILE811

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:PRU10027
ChainResidueDetails
AASP803
BASP803

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159
ChainResidueDetails
ALEU686
BLEU686

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING:
ChainResidueDetails
ALYS709
BLYS709

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: Phosphotyrosine => ECO:0000269|PubMed:16407264
ChainResidueDetails
ATYR718
BTYR718

site_idSWS_FT_FI5
Number of Residues4
DetailsMOD_RES: Phosphothreonine; by autocatalysis => ECO:0000269|PubMed:17937911
ChainResidueDetails
ATHR813
ATHR842
BTHR813
BTHR842

site_idSWS_FT_FI6
Number of Residues2
DetailsMOD_RES: Phosphothreonine; by autocatalysis, MELK and MAP3K6 => ECO:0000269|PubMed:11920685, ECO:0000269|PubMed:17210579, ECO:0000269|PubMed:17937911, ECO:0000269|PubMed:18948261, ECO:0000269|PubMed:19590015, ECO:0000269|PubMed:23102700
ChainResidueDetails
AGLU838
BGLU838

site_idSWS_FT_FI7
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163
ChainResidueDetails
ASER958
BSER958

site_idSWS_FT_FI8
Number of Residues2
DetailsMOD_RES: Phosphoserine; by autocatalysis => ECO:0000269|PubMed:14688258, ECO:0000269|PubMed:15094778, ECO:0000269|PubMed:19590015, ECO:0000269|PubMed:26095851
ChainResidueDetails
ASER966
BSER966

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PDB entries from 2024-05-29

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