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1ZMR

Crystal Structure of the E. coli Phosphoglycerate Kinase

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0004618molecular_functionphosphoglycerate kinase activity
A0005524molecular_functionATP binding
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006094biological_processgluconeogenesis
A0006096biological_processglycolytic process
A0016301molecular_functionkinase activity
A0016740molecular_functiontransferase activity
A0043531molecular_functionADP binding
A0097216molecular_functionguanosine tetraphosphate binding
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA A 401
ChainResidue
AASP237
AASP240
AGLU383
ALYS386
AHOH491

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CA A 402
ChainResidue
ALYS84
AHOH510
AHOH546
AHOH564

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CA A 403
ChainResidue
ALYS82
ALEU85
AGLU323
AHOH531

Functional Information from PROSITE/UniProt
site_idPS00111
Number of Residues11
DetailsPGLYCERATE_KINASE Phosphoglycerate kinase signature. RVFIRaDlNVP
ChainResidueDetails
AARG15-PRO25

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues13
DetailsBinding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues1
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"18723842","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues4
DetailsAnnotated By Reference To The Literature 13pk
ChainResidueDetails
AGLY364
ALYS193
AGLY341
AARG36

249697

PDB entries from 2026-02-25

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