Structure of PDB 4o33 Chain A Binding Site BS01

Receptor Information
>4o33 Chain A (length=417) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
MSLSNKLTLDKLDVKGKRVVMRVDFNVPMKNNQITNNQRIKAAVPSIKFC
LDNGAKSVVLMSHLGRPDGVPMPDKYSLEPVAVELKSLLGKDVLFLKDCV
GPEVEKACANPAAGSVILLENLRFHVEEEGKGKDASGNKVKAEPAKIEAF
RASLSKLGDVYVNDAFGTAHRAHSSMVGVNLPQKAGGFLMKKELNYFAKA
LESPERPFLAILGGAKVADKIQLINNMLDKVNEMIIGGGMAFTFLKVLNN
MEIGTSLFDEEGAKIVKDLMSKAEKNGVKITLPVDFVTADKFDENAKTGQ
ATVASGIPAGWMGLDCGPESSKKYAEAVTRAKQIVWNGPVGVFEWEAFAR
GTKALMDEVVKATSRGCITTIGGGDTATCCAKWNTEDKVSHVSTGGGASL
ELLEGKVLPGVDALSNI
Ligand information
Ligand IDTZN
InChIInChI=1S/C19H25N5O4/c1-26-15-10-12-13(11-16(15)27-2)21-19(22-17(12)20)24-7-5-23(6-8-24)18(25)14-4-3-9-28-14/h10-11,14H,3-9H2,1-2H3,(H2,20,21,22)/t14-/m1/s1
InChIKeyVCKUSRYTPJJLNI-CQSZACIVSA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.7.6COc1cc2c(cc1OC)nc(nc2N)N3CCN(CC3)C(=O)C4CCCO4
OpenEye OEToolkits 1.7.6COc1cc2c(cc1OC)nc(nc2N)N3CCN(CC3)C(=O)[C@H]4CCCO4
CACTVS 3.385COc1cc2nc(nc(N)c2cc1OC)N3CCN(CC3)C(=O)[CH]4CCCO4
CACTVS 3.385COc1cc2nc(nc(N)c2cc1OC)N3CCN(CC3)C(=O)[C@H]4CCCO4
ACDLabs 12.01O=C(N3CCN(c2nc1cc(OC)c(OC)cc1c(n2)N)CC3)C4OCCC4
FormulaC19 H25 N5 O4
Name[4-(4-amino-6,7-dimethoxyquinazolin-2-yl)piperazin-1-yl][(2R)-tetrahydrofuran-2-yl]methanone;
Terazosin
ChEMBLCHEMBL1481149
DrugBank
ZINCZINC000095616600
PDB chain4o33 Chain A Residue 501 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB4o33 Terazosin activates Pgk1 and Hsp90 to promote stress resistance.
Resolution2.1 Å
Binding residue
(original residue number in PDB)		G237 G238 T254 L256 F291 M311 G312 L313 G340 V341
Binding residue
(residue number reindexed from 1)		G238 G239 T255 L257 F292 M312 G313 L314 G341 V342
Annotation score1
Binding affinityMOAD: Kd=2.78uM
Enzymatic activity
Catalytic site (original residue number in PDB) R38 K215 G373 G396
Catalytic site (residue number reindexed from 1) R39 K216 G374 G397
Enzyme Commision number 2.7.2.3: phosphoglycerate kinase.
Gene Ontology
Molecular Function
GO:0004618 phosphoglycerate kinase activity
GO:0005515 protein binding
GO:0005524 ATP binding
GO:0016301 kinase activity
GO:0043531 ADP binding
GO:0047134 protein-disulfide reductase (NAD(P)H) activity
Biological Process
GO:0006094 gluconeogenesis
GO:0006096 glycolytic process
GO:0016310 phosphorylation
GO:0016525 negative regulation of angiogenesis
GO:0030855 epithelial cell differentiation
GO:0031639 plasminogen activation
GO:0061621 canonical glycolysis
GO:0071456 cellular response to hypoxia
Cellular Component
GO:0005615 extracellular space
GO:0005737 cytoplasm
GO:0005829 cytosol
GO:0016020 membrane
GO:0045121 membrane raft
GO:0070062 extracellular exosome

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:4o33, PDBe:4o33, PDBj:4o33
PDBsum4o33
PubMed25383758
UniProtP00558|PGK1_HUMAN Phosphoglycerate kinase 1 (Gene Name=PGK1)

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