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4O33

Crystal Structure of human PGK1 3PG and terazosin(TZN) ternary complex

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0004618molecular_functionphosphoglycerate kinase activity
A0005515molecular_functionprotein binding
A0005524molecular_functionATP binding
A0005615cellular_componentextracellular space
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006094biological_processgluconeogenesis
A0006096biological_processglycolytic process
A0016020cellular_componentmembrane
A0016301molecular_functionkinase activity
A0016310biological_processphosphorylation
A0016525biological_processnegative regulation of angiogenesis
A0016740molecular_functiontransferase activity
A0030855biological_processepithelial cell differentiation
A0031639biological_processplasminogen activation
A0043531molecular_functionADP binding
A0045121cellular_componentmembrane raft
A0047134molecular_functionprotein-disulfide reductase (NAD(P)H) activity
A0061621biological_processcanonical glycolysis
A0070062cellular_componentextracellular exosome
A0071456biological_processcellular response to hypoxia
Functional Information from PDB Data
site_idAC1
Number of Residues13
DetailsBINDING SITE FOR RESIDUE TZN A 501
ChainResidue
AGLY237
APRO338
AGLY340
AVAL341
AHOH609
AGLY238
ATHR254
ALEU256
APHE291
AMET311
AGLY312
ALEU313
AASP314

site_idAC2
Number of Residues12
DetailsBINDING SITE FOR RESIDUE 3PG A 502
ChainResidue
AASP23
AASN25
AARG38
AHIS62
AARG65
AARG122
AGLY166
ATHR167
AARG170
AHOH705
AHOH707
AHOH784

Functional Information from PROSITE/UniProt
site_idPS00111
Number of Residues11
DetailsPGLYCERATE_KINASE Phosphoglycerate kinase signature. RVVMRvDfNVP
ChainResidueDetails
AARG17-PRO27

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues9
DetailsBINDING: BINDING => ECO:0000269|PubMed:18463139
ChainResidueDetails
AASP23
AARG38
AHIS62
AARG122
AARG170
ALYS219
AGLY312
AGLU343
AGLY372

site_idSWS_FT_FI2
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163
ChainResidueDetails
ASER1
ASER3

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:P09411
ChainResidueDetails
ALYS5
ALYS190

site_idSWS_FT_FI4
Number of Residues7
DetailsMOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861
ChainResidueDetails
ALYS10
ALYS74
ALYS85
ALYS145
ALYS198
ALYS266
ALYS290

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P09411
ChainResidueDetails
ALYS47

site_idSWS_FT_FI6
Number of Residues1
DetailsMOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:P09411
ChainResidueDetails
ATYR75

site_idSWS_FT_FI7
Number of Residues2
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P09411
ChainResidueDetails
ALYS90
ALYS360

site_idSWS_FT_FI8
Number of Residues1
DetailsMOD_RES: N6-acetyllysine; alternate => ECO:0007744|PubMed:19608861
ChainResidueDetails
ALYS96

site_idSWS_FT_FI9
Number of Residues1
DetailsMOD_RES: N6-malonyllysine; alternate => ECO:0000269|PubMed:21908771
ChainResidueDetails
ALYS130

site_idSWS_FT_FI10
Number of Residues1
DetailsMOD_RES: Phosphotyrosine => ECO:0007744|PubMed:15592455
ChainResidueDetails
ATYR195

site_idSWS_FT_FI11
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569
ChainResidueDetails
ASER202

site_idSWS_FT_FI12
Number of Residues2
DetailsMOD_RES: N6-(2-hydroxyisobutyryl)lysine => ECO:0000269|PubMed:29775581
ChainResidueDetails
ALYS215
ALYS322

site_idSWS_FT_FI13
Number of Residues1
DetailsMOD_RES: N6-(2-hydroxyisobutyryl)lysine => ECO:0000269|PubMed:29192674
ChainResidueDetails
ALYS219

218853

PDB entries from 2024-04-24

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