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3VW6

Crystal structure of human apoptosis signal-regulating kinase 1 (ASK1) with imidazopyridine inhibitor

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 Residues11
DetailsBINDING SITE FOR RESIDUE IM6 A 1001
ChainResidue
AVAL694
ATYR814
ASER821
ALYS709
AMET754
AGLU755
AGLN756
AVAL757
AGLY759
AGLY760
ALEU810

site_idAC2
Number of Residues10
DetailsBINDING SITE FOR RESIDUE IM6 B 1001
ChainResidue
BALA707
BLYS709
BMET754
BGLU755
BGLN756
BVAL757
BGLY759
BGLY760
BLEU810
BTYR814

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
BASP803
AASP803

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
ATHR838
BTHR838

221051

PDB entries from 2024-06-12

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