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5M1R

X-ray structure of human G166D PGK-1 mutant

Functional Information from GO Data
ChainGOidnamespacecontents
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
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 Residues24
Detailsbinding site for residue ADP A 501
ChainResidue
AGLY213
ALEU313
AASN336
AGLY337
AGLY340
AVAL341
AGLU343
AASP374
ATHR375
AMG502
AHOH603
AALA214
AHOH634
AHOH654
AHOH700
AHOH736
AHOH765
ALYS215
AASP218
ALYS219
AGLY237
AGLY238
ALEU256
AGLY312

site_idAC2
Number of Residues6
Detailsbinding site for residue MG A 502
ChainResidue
AASN336
AGLY372
AASP374
ATHR375
AADP501
AHOH608

site_idAC3
Number of Residues5
Detailsbinding site for residue MG A 503
ChainResidue
ALYS85
AARG150
AALA151
AHOH605
AHOH810

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
AARG38
AHIS62
AARG122
AARG170
ALYS219
AGLY312
AGLU343
AGLY372
AASP23

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
ALYS74
ALYS85
ALYS145
ALYS198
ALYS266
ALYS290
ALYS10

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
ALYS322
ALYS215

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

220472

PDB entries from 2024-05-29

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