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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

1IAT

CRYSTAL STRUCTURE OF HUMAN PHOSPHOGLUCOSE ISOMERASE/NEUROLEUKIN/AUTOCRINE MOTILITY FACTOR/MATURATION FACTOR

Functional Information from GO Data
ChainGOidnamespacecontents
A0002639biological_processpositive regulation of immunoglobulin production
A0004347molecular_functionglucose-6-phosphate isomerase activity
A0005125molecular_functioncytokine activity
A0005515molecular_functionprotein binding
A0005576cellular_componentextracellular region
A0005615cellular_componentextracellular space
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0005975biological_processcarbohydrate metabolic process
A0006002biological_processfructose 6-phosphate metabolic process
A0006094biological_processgluconeogenesis
A0006096biological_processglycolytic process
A0006959biological_processhumoral immune response
A0007165biological_processsignal transduction
A0007599biological_processhemostasis
A0007611biological_processlearning or memory
A0008083molecular_functiongrowth factor activity
A0010595biological_processpositive regulation of endothelial cell migration
A0016020cellular_componentmembrane
A0016853molecular_functionisomerase activity
A0016857molecular_functionracemase and epimerase activity, acting on carbohydrates and derivatives
A0031625molecular_functionubiquitin protein ligase binding
A0032355biological_processresponse to estradiol
A0032570biological_processresponse to progesterone
A0033574biological_processresponse to testosterone
A0034774cellular_componentsecretory granule lumen
A0035902biological_processresponse to immobilization stress
A0035994biological_processresponse to muscle stretch
A0043066biological_processnegative regulation of apoptotic process
A0046686biological_processresponse to cadmium ion
A0047938molecular_functionglucose-6-phosphate 1-epimerase activity
A0048029molecular_functionmonosaccharide binding
A0051156biological_processglucose 6-phosphate metabolic process
A0070062cellular_componentextracellular exosome
A0097367molecular_functioncarbohydrate derivative binding
A1901135biological_processcarbohydrate derivative metabolic process
A1904813cellular_componentficolin-1-rich granule lumen
Functional Information from PDB Data
site_idAC1
Number of Residues10
DetailsBINDING SITE FOR RESIDUE SO4 A 602
ChainResidue
ASER159
AHOH973
ASER209
ALYS210
ATHR211
ATHR214
ABME601
AHOH627
AHOH747
AHOH925
site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SO4 A 603
ChainResidue
AARG27
AASN46
AHIS47
AHOH985
AHOH1056
AHOH1070
AHOH1161
site_idAC3
Number of Residues8
DetailsBINDING SITE FOR RESIDUE BME A 601
ChainResidue
AGLY158
AGLY271
AGLN353
ASO4602
AHOH710
AHOH747
AHOH866
AHOH973
Functional Information from PROSITE/UniProt
site_idPS00174
Number of Residues18
DetailsP_GLUCOSE_ISOMERASE_2 Phosphoglucose isomerase signature 2. GiIWdinsFDQwGVElgK
ChainResidueDetails
AGLY501-LYS518
site_idPS00765
Number of Residues14
DetailsP_GLUCOSE_ISOMERASE_1 Phosphoglucose isomerase signature 1. DwVGGRYSLwSAIG
ChainResidueDetails
AASP267-GLY280
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsActive site: {"description":"Proton donor","evidences":[{"source":"PubMed","id":"11371164","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12573240","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12777791","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues2
DetailsActive site: {"evidences":[{"source":"PubMed","id":"11371164","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12573240","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12777791","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues10
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"P06745","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues1
DetailsModified residue: {"description":"N-acetylalanine","evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"OCT-2004","submissionDatabase":"UniProtKB","authors":["Bienvenut W.V."]}},{"source":"PubMed","id":"19413330","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues2
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues1
DetailsModified residue: {"description":"N6-(2-hydroxyisobutyryl)lysine","evidences":[{"source":"PubMed","id":"29775581","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI8
Number of Residues1
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"18669648","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"19690332","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI9
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine; by CK2","evidences":[{"source":"PubMed","id":"11004567","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15637053","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI10
Number of Residues1
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"Q6P6V0","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI11
Number of Residues1
DetailsModified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P06745","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
Catalytic Information from CSA
site_idCSA1
Number of Residues6
DetailsAnnotated By Reference To The Literature 1dqr
ChainResidueDetails
AARG272
ALYS518
AGLU216
AGLU357
ALYS210
AGLY271
site_idCSA2
Number of Residues1
DetailsAnnotated By Reference To The Literature 1dqr
ChainResidueDetails
AHIS388

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PDB entries from 2025-12-24

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