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2CXR

Crystal structure of mouse AMF / 6PG complex

Functional Information from GO Data
ChainGOidnamespacecontents
A0001701biological_processin utero embryonic development
A0001707biological_processmesoderm formation
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
A0005886cellular_componentplasma membrane
A0006002biological_processfructose 6-phosphate metabolic process
A0006094biological_processgluconeogenesis
A0006096biological_processglycolytic process
A0007165biological_processsignal transduction
A0007611biological_processlearning or memory
A0008083molecular_functiongrowth factor activity
A0010595biological_processpositive regulation of endothelial cell migration
A0016853molecular_functionisomerase activity
A0031625molecular_functionubiquitin protein ligase binding
A0032355biological_processresponse to estradiol
A0032570biological_processresponse to progesterone
A0033574biological_processresponse to testosterone
A0034101biological_processerythrocyte homeostasis
A0035902biological_processresponse to immobilization stress
A0035994biological_processresponse to muscle stretch
A0042593biological_processglucose homeostasis
A0043066biological_processnegative regulation of apoptotic process
A0043209cellular_componentmyelin sheath
A0046686biological_processresponse to cadmium ion
A0048029molecular_functionmonosaccharide binding
A0051156biological_processglucose 6-phosphate metabolic process
A0060170cellular_componentciliary membrane
A0061615biological_processglycolytic process through fructose-6-phosphate
A0061620biological_processglycolytic process through glucose-6-phosphate
A0061621biological_processcanonical glycolysis
A0097367molecular_functioncarbohydrate derivative binding
A1901135biological_processcarbohydrate derivative metabolic process
A1904539biological_processnegative regulation of glycolytic process through fructose-6-phosphate
A1904540biological_processpositive regulation of glycolytic process through fructose-6-phosphate
B0001701biological_processin utero embryonic development
B0001707biological_processmesoderm formation
B0002639biological_processpositive regulation of immunoglobulin production
B0004347molecular_functionglucose-6-phosphate isomerase activity
B0005125molecular_functioncytokine activity
B0005515molecular_functionprotein binding
B0005576cellular_componentextracellular region
B0005615cellular_componentextracellular space
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0005886cellular_componentplasma membrane
B0006002biological_processfructose 6-phosphate metabolic process
B0006094biological_processgluconeogenesis
B0006096biological_processglycolytic process
B0007165biological_processsignal transduction
B0007611biological_processlearning or memory
B0008083molecular_functiongrowth factor activity
B0010595biological_processpositive regulation of endothelial cell migration
B0016853molecular_functionisomerase activity
B0031625molecular_functionubiquitin protein ligase binding
B0032355biological_processresponse to estradiol
B0032570biological_processresponse to progesterone
B0033574biological_processresponse to testosterone
B0034101biological_processerythrocyte homeostasis
B0035902biological_processresponse to immobilization stress
B0035994biological_processresponse to muscle stretch
B0042593biological_processglucose homeostasis
B0043066biological_processnegative regulation of apoptotic process
B0043209cellular_componentmyelin sheath
B0046686biological_processresponse to cadmium ion
B0048029molecular_functionmonosaccharide binding
B0051156biological_processglucose 6-phosphate metabolic process
B0060170cellular_componentciliary membrane
B0061615biological_processglycolytic process through fructose-6-phosphate
B0061620biological_processglycolytic process through glucose-6-phosphate
B0061621biological_processcanonical glycolysis
B0097367molecular_functioncarbohydrate derivative binding
B1901135biological_processcarbohydrate derivative metabolic process
B1904539biological_processnegative regulation of glycolytic process through fructose-6-phosphate
B1904540biological_processpositive regulation of glycolytic process through fructose-6-phosphate
Functional Information from PDB Data
site_idAC1
Number of Residues22
DetailsBINDING SITE FOR RESIDUE 6PG A 1601
ChainResidue
AILE157
AARG273
AGLN354
AGLU358
AGLN512
ALYS519
AHOH1709
AHOH1757
AHOH1764
AHOH1774
AHOH1778
AGLY158
AHOH1853
AHOH1911
BHIS389
AGLY159
ASER160
ASER210
ALYS211
ATHR212
ATHR215
AGLY272

site_idAC2
Number of Residues22
DetailsBINDING SITE FOR RESIDUE 6PG B 2601
ChainResidue
AHIS389
BILE157
BGLY159
BSER160
BSER210
BLYS211
BTHR212
BTHR215
BGLY272
BARG273
BGLN354
BGLU358
BGLN512
BHOH2643
BHOH2657
BHOH2684
BHOH2705
BHOH2748
BHOH2766
BHOH2775
BHOH2812
BHOH2920

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL A 1701
ChainResidue
AASP140
ATRP141
ALYS142
ALYS241
AHOH1918
AHOH2064

site_idAC4
Number of Residues8
DetailsBINDING SITE FOR RESIDUE GOL A 1702
ChainResidue
AILE549
AARG553
AHOH1823
AHOH1887
BGLY419
BHIS422
BLYS423
BLEU426

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE GOL B 1703
ChainResidue
BARG135
BTRP141
BLYS142
BHOH2810

site_idAC6
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL A 1704
ChainResidue
AGLY419
AHIS422
ALYS423
ALEU426
AHOH1873
AHOH1882
BARG553

Functional Information from PROSITE/UniProt
site_idPS00174
Number of Residues18
DetailsP_GLUCOSE_ISOMERASE_2 Phosphoglucose isomerase signature 2. GiMWdinsFDQwGVElgK
ChainResidueDetails
AGLY502-LYS519

site_idPS00765
Number of Residues14
DetailsP_GLUCOSE_ISOMERASE_1 Phosphoglucose isomerase signature 1. DwVGGRYSLwSAIG
ChainResidueDetails
AASP268-GLY281

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsActive site: {"description":"Proton donor","evidences":[{"source":"PubMed","id":"15342241","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues4
DetailsActive site: {"evidences":[{"source":"PubMed","id":"15342241","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues20
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"15342241","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16375918","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1U0F","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2CXS","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2CXT","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues2
DetailsModified residue: {"description":"N-acetylalanine","evidences":[{"source":"UniProtKB","id":"P06744","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues2
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P06744","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"Q6P6V0","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P06744","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues2
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"P06744","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues2
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"23806337","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine; by CK2","evidences":[{"source":"UniProtKB","id":"P06744","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI11
Number of Residues2
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"Q6P6V0","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI12
Number of Residues2
DetailsModified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"PubMed","id":"23806337","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI13
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"21183079","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues7
DetailsAnnotated By Reference To The Literature 1dqr
ChainResidueDetails
AHIS389
BGLY272
BARG273
BLYS211
BGLU358
BLYS519
BGLU217

site_idCSA2
Number of Residues7
DetailsAnnotated By Reference To The Literature 1dqr
ChainResidueDetails
AGLY272
AARG273
ALYS211
ALYS519
AGLU358
AGLU217
BHIS389

239492

PDB entries from 2025-07-30

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