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2CXN

Crystal structure of mouse AMF / phosphate 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
A0043209cellular_componentmyelin sheath
A0043524biological_processnegative regulation of neuron apoptotic process
A0046686biological_processresponse to cadmium ion
A0048029molecular_functionmonosaccharide binding
A0051156biological_processglucose 6-phosphate metabolic process
A0060170cellular_componentciliary membrane
A0061620biological_processglycolytic process through glucose-6-phosphate
A0061621biological_processcanonical glycolysis
A0097367molecular_functioncarbohydrate derivative binding
A1901135biological_processcarbohydrate derivative metabolic process
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
B0043209cellular_componentmyelin sheath
B0043524biological_processnegative regulation of neuron apoptotic process
B0046686biological_processresponse to cadmium ion
B0048029molecular_functionmonosaccharide binding
B0051156biological_processglucose 6-phosphate metabolic process
B0060170cellular_componentciliary membrane
B0061620biological_processglycolytic process through glucose-6-phosphate
B0061621biological_processcanonical glycolysis
B0097367molecular_functioncarbohydrate derivative binding
B1901135biological_processcarbohydrate derivative metabolic process
Functional Information from PDB Data
site_idAC1
Number of Residues9
DetailsBINDING SITE FOR RESIDUE PO4 A 1601
ChainResidue
ASER160
ASER210
ALYS211
ATHR212
ATHR215
AHOH1707
AHOH1847
AHOH1916
AHOH1995

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL A 1701
ChainResidue
AASP140
ATRP141
ALYS142
ALYS241
AHOH1950
AHOH2302

site_idAC3
Number of Residues8
DetailsBINDING SITE FOR RESIDUE GOL B 1702
ChainResidue
AILE549
AARG553
BGLY419
BHIS422
BLYS423
BLEU426
BHOH1926
BHOH1947

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE GOL B 1703
ChainResidue
BARG135
BTRP141
BLYS142
BHOH1857

site_idAC5
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL A 1704
ChainResidue
AGLY419
AHIS422
ALYS423
ALEU426
AHOH1839
AHOH1956
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
DetailsACT_SITE: Proton donor => ECO:0000269|PubMed:15342241
ChainResidueDetails
ASER359
BSER359

site_idSWS_FT_FI2
Number of Residues4
DetailsACT_SITE: ACT_SITE => ECO:0000269|PubMed:15342241
ChainResidueDetails
AALA390
AGLN520
BALA390
BGLN520

site_idSWS_FT_FI3
Number of Residues12
DetailsBINDING: BINDING => ECO:0000269|PubMed:15342241, ECO:0000269|PubMed:16375918, ECO:0007744|PDB:1U0F, ECO:0007744|PDB:2CXS, ECO:0007744|PDB:2CXT
ChainResidueDetails
ASER160
BSER359
BALA390
BGLN520
ALYS211
AGLY355
ASER359
AALA390
AGLN520
BSER160
BLYS211
BGLY355

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: N-acetylalanine => ECO:0000250|UniProtKB:P06744
ChainResidueDetails
AALA3
BALA3

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P06744
ChainResidueDetails
ALEU13
BLEU13

site_idSWS_FT_FI6
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q6P6V0
ChainResidueDetails
AGLY87
BGLY87

site_idSWS_FT_FI7
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P06744
ChainResidueDetails
AASN108
BASN108

site_idSWS_FT_FI8
Number of Residues2
DetailsMOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:P06744
ChainResidueDetails
APRO110
BPRO110

site_idSWS_FT_FI9
Number of Residues2
DetailsMOD_RES: N6-acetyllysine => ECO:0007744|PubMed:23806337
ChainResidueDetails
AGLY143
BGLY143

site_idSWS_FT_FI10
Number of Residues2
DetailsMOD_RES: Phosphoserine; by CK2 => ECO:0000250|UniProtKB:P06744
ChainResidueDetails
AASN186
BASN186

site_idSWS_FT_FI11
Number of Residues2
DetailsMOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:Q6P6V0
ChainResidueDetails
AALA251
BALA251

site_idSWS_FT_FI12
Number of Residues2
DetailsMOD_RES: N6-succinyllysine; alternate => ECO:0007744|PubMed:23806337
ChainResidueDetails
ASER455
BSER455

site_idSWS_FT_FI13
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:21183079
ChainResidueDetails
APRO456
BPRO456

218853

PDB entries from 2024-04-24

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