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3ZOZ

The structure of human phosphoglycerate kinase with bound bromide, a stimulating anion.

Functional Information from GO Data
ChainGOidnamespacecontents
A0004618molecular_functionphosphoglycerate kinase activity
A0004674molecular_functionprotein serine/threonine kinase activity
A0005515molecular_functionprotein binding
A0005524molecular_functionATP binding
A0005615cellular_componentextracellular space
A0005737cellular_componentcytoplasm
A0005759cellular_componentmitochondrial matrix
A0005829cellular_componentcytosol
A0006094biological_processgluconeogenesis
A0006096biological_processglycolytic process
A0016020cellular_componentmembrane
A0016301molecular_functionkinase activity
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
A0160218
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG A 1418
ChainResidue
AASP375
AMGF1420
AADP1422
AHOH2241
AHOH2400

site_idAC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE BR A 1419
ChainResidue
AARG66
ALYS216
AASP219

site_idAC3
Number of Residues13
DetailsBINDING SITE FOR RESIDUE MGF A 1420
ChainResidue
ALYS216
ALYS220
AGLY373
AGLY374
AGLY396
AGLY397
AMG1418
A3PG1421
AADP1422
AHOH2197
AHOH2241
AHOH2400
AARG39

site_idAC4
Number of Residues15
DetailsBINDING SITE FOR RESIDUE 3PG A 1421
ChainResidue
AASP24
AASN26
AARG39
AHIS63
AARG66
AARG123
AGLY167
AARG171
ALYS216
AMGF1420
AHOH2049
AHOH2167
AHOH2194
AHOH2197
AHOH2400

site_idAC5
Number of Residues30
DetailsBINDING SITE FOR RESIDUE ADP A 1422
ChainResidue
AGLY214
AALA215
ALYS216
ALYS220
AGLY238
AGLY239
ALEU257
AGLY313
ALEU314
AASN337
APRO339
AGLY341
AVAL342
AGLU344
AGLY372
AGLY373
AGLY374
AASP375
ATHR376
AMG1418
AMGF1420
AHOH2240
AHOH2241
AHOH2291
AHOH2358
AHOH2398
AHOH2400
AHOH2427
AHOH2428
AHOH2429

Functional Information from PROSITE/UniProt
site_idPS00111
Number of Residues11
DetailsPGLYCERATE_KINASE Phosphoglycerate kinase signature. RVVMRvDfNVP
ChainResidueDetails
AARG18-PRO28

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues9
DetailsBINDING: BINDING => ECO:0000269|PubMed:18463139
ChainResidueDetails
AASP24
AARG39
AHIS63
AARG123
AARG171
ALYS220
AGLY313
AGLU344
AGLY373

site_idSWS_FT_FI2
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163
ChainResidueDetails
ASER2
ASER4

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:P09411
ChainResidueDetails
ALYS6
ALYS191

site_idSWS_FT_FI4
Number of Residues7
DetailsMOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861
ChainResidueDetails
ALYS11
ALYS75
ALYS86
ALYS146
ALYS199
ALYS267
ALYS291

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P09411
ChainResidueDetails
ALYS48

site_idSWS_FT_FI6
Number of Residues1
DetailsMOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:P09411
ChainResidueDetails
ATYR76

site_idSWS_FT_FI7
Number of Residues2
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P09411
ChainResidueDetails
ALYS91
ALYS361

site_idSWS_FT_FI8
Number of Residues1
DetailsMOD_RES: N6-acetyllysine; alternate => ECO:0007744|PubMed:19608861
ChainResidueDetails
ALYS97

site_idSWS_FT_FI9
Number of Residues1
DetailsMOD_RES: N6-malonyllysine; alternate => ECO:0000269|PubMed:21908771
ChainResidueDetails
ALYS131

site_idSWS_FT_FI10
Number of Residues1
DetailsMOD_RES: Phosphotyrosine => ECO:0007744|PubMed:15592455
ChainResidueDetails
ATYR196

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
ASER203

site_idSWS_FT_FI12
Number of Residues2
DetailsMOD_RES: N6-(2-hydroxyisobutyryl)lysine => ECO:0000269|PubMed:29775581
ChainResidueDetails
ALYS216
ALYS323

site_idSWS_FT_FI13
Number of Residues1
DetailsMOD_RES: N6-(2-hydroxyisobutyryl)lysine => ECO:0000269|PubMed:29192674
ChainResidueDetails
ALYS220

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PDB entries from 2024-11-06

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