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6RNG

Dipeptide Gly-Pro binds to a glycolytic enzyme fructose bisphosphate aldolase

Functional Information from GO Data
ChainGOidnamespacecontents
A0003729molecular_functionmRNA binding
A0004332molecular_functionfructose-bisphosphate aldolase activity
A0005507molecular_functioncopper ion binding
A0005515molecular_functionprotein binding
A0005634cellular_componentnucleus
A0005737cellular_componentcytoplasm
A0005739cellular_componentmitochondrion
A0005783cellular_componentendoplasmic reticulum
A0005829cellular_componentcytosol
A0005886cellular_componentplasma membrane
A0006094biological_processgluconeogenesis
A0006096biological_processglycolytic process
A0009506cellular_componentplasmodesma
A0016829molecular_functionlyase activity
A0030388biological_processfructose 1,6-bisphosphate metabolic process
A0031930biological_processmitochondria-nucleus signaling pathway
A0071456biological_processcellular response to hypoxia
A1901149molecular_functionsalicylic acid binding
B0003729molecular_functionmRNA binding
B0004332molecular_functionfructose-bisphosphate aldolase activity
B0005507molecular_functioncopper ion binding
B0005515molecular_functionprotein binding
B0005634cellular_componentnucleus
B0005737cellular_componentcytoplasm
B0005739cellular_componentmitochondrion
B0005783cellular_componentendoplasmic reticulum
B0005829cellular_componentcytosol
B0005886cellular_componentplasma membrane
B0006094biological_processgluconeogenesis
B0006096biological_processglycolytic process
B0009506cellular_componentplasmodesma
B0016829molecular_functionlyase activity
B0030388biological_processfructose 1,6-bisphosphate metabolic process
B0031930biological_processmitochondria-nucleus signaling pathway
B0071456biological_processcellular response to hypoxia
B1901149molecular_functionsalicylic acid binding
F0003729molecular_functionmRNA binding
F0004332molecular_functionfructose-bisphosphate aldolase activity
F0005507molecular_functioncopper ion binding
F0005515molecular_functionprotein binding
F0005634cellular_componentnucleus
F0005737cellular_componentcytoplasm
F0005739cellular_componentmitochondrion
F0005783cellular_componentendoplasmic reticulum
F0005829cellular_componentcytosol
F0005886cellular_componentplasma membrane
F0006094biological_processgluconeogenesis
F0006096biological_processglycolytic process
F0009506cellular_componentplasmodesma
F0016829molecular_functionlyase activity
F0030388biological_processfructose 1,6-bisphosphate metabolic process
F0031930biological_processmitochondria-nucleus signaling pathway
F0071456biological_processcellular response to hypoxia
F1901149molecular_functionsalicylic acid binding
G0003729molecular_functionmRNA binding
G0004332molecular_functionfructose-bisphosphate aldolase activity
G0005507molecular_functioncopper ion binding
G0005515molecular_functionprotein binding
G0005634cellular_componentnucleus
G0005737cellular_componentcytoplasm
G0005739cellular_componentmitochondrion
G0005783cellular_componentendoplasmic reticulum
G0005829cellular_componentcytosol
G0005886cellular_componentplasma membrane
G0006094biological_processgluconeogenesis
G0006096biological_processglycolytic process
G0009506cellular_componentplasmodesma
G0016829molecular_functionlyase activity
G0030388biological_processfructose 1,6-bisphosphate metabolic process
G0031930biological_processmitochondria-nucleus signaling pathway
G0071456biological_processcellular response to hypoxia
G1901149molecular_functionsalicylic acid binding
Functional Information from PDB Data
site_idAC1
Number of Residues6
Detailsbinding site for residue SO4 A 401
ChainResidue
AGLN156
AARG203
ALYS210
AASP214
AHOH548
BGLN156

site_idAC2
Number of Residues8
Detailsbinding site for residue SO4 B 401
ChainResidue
BILE159
BARG203
BALA207
BLYS210
BHOH501
AGLN156
AHOH526
BGLN156

site_idAC3
Number of Residues1
Detailsbinding site for residue SO4 B 402
ChainResidue
BARG253

site_idAC4
Number of Residues4
Detailsbinding site for residue SO4 B 403
ChainResidue
BSER32
BTHR35
BLYS103
BHOH507

site_idAC5
Number of Residues6
Detailsbinding site for residue SO4 B 404
ChainResidue
ALYS288
AHOH513
AHOH540
BLYS285
BHOH521
BHOH534

site_idAC6
Number of Residues4
Detailsbinding site for residue SO4 B 405
ChainResidue
BGLU11
BLYS94
BARG139
BHOH522

site_idAC7
Number of Residues6
Detailsbinding site for residue SO4 B 406
ChainResidue
AGLN156
AARG203
BGLN156
BARG203
BHOH516
BHOH549

site_idAC8
Number of Residues3
Detailsbinding site for residue GLY B 407
ChainResidue
BGLY267
BARG298
BPRO408

site_idAC9
Number of Residues6
Detailsbinding site for residue PRO B 408
ChainResidue
BLEU265
BSER266
BGLY267
BARG298
BGLY407
BHOH548

site_idAD1
Number of Residues8
Detailsbinding site for residue SO4 F 401
ChainResidue
FGLN156
FILE159
FARG203
FALA207
FLYS210
FASP214
FHOH551
GGLN156

site_idAD2
Number of Residues5
Detailsbinding site for residue SO4 F 402
ChainResidue
FASP30
FSER32
FTHR35
FLYS103
FHOH520

site_idAD3
Number of Residues9
Detailsbinding site for residue SO4 G 401
ChainResidue
FGLN156
GGLN156
GILE159
GARG203
GALA207
GLYS210
GASP214
GHOH512
GHOH560

site_idAD4
Number of Residues6
Detailsbinding site for residue SO4 G 402
ChainResidue
GASP30
GGLU31
GSER32
GTHR35
GLYS103
GHOH537

site_idAD5
Number of Residues3
Detailsbinding site for residue SO4 G 403
ChainResidue
FLYS288
FHOH529
GLYS285

site_idAD6
Number of Residues5
Detailsbinding site for residue SO4 G 404
ChainResidue
FLYS327
GGLU11
GLYS94
GARG139
GHOH572

site_idAD7
Number of Residues5
Detailsbinding site for residue GLY G 405
ChainResidue
GSER266
GGLY267
GARG298
GPRO406
GHOH556

site_idAD8
Number of Residues8
Detailsbinding site for residue PRO G 406
ChainResidue
GARG39
GLYS225
GSER266
GSER295
GGLY297
GARG298
GGLY405
GHOH552

site_idAD9
Number of Residues4
Detailsbinding site for residue GLY G 407
ChainResidue
FGLY64
FCYS68
FLYS327
GPRO408

site_idAE1
Number of Residues3
Detailsbinding site for residue PRO G 408
ChainResidue
GHOH546
GASN15
GGLY407

Functional Information from PROSITE/UniProt
site_idPS00158
Number of Residues11
DetailsALDOLASE_CLASS_I Fructose-bisphosphate aldolase class-I active site. VlLEGtLLKPN
ChainResidueDetails
AVAL217-ASN227

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsACT_SITE: Proton acceptor => ECO:0000250|UniProtKB:P00883
ChainResidueDetails
AGLU183
BGLU183
FGLU183
GGLU183

site_idSWS_FT_FI2
Number of Residues4
DetailsACT_SITE: Schiff-base intermediate with dihydroxyacetone-P => ECO:0000250|UniProtKB:P00883
ChainResidueDetails
ALYS225
BLYS225
FLYS225
GLYS225

site_idSWS_FT_FI3
Number of Residues12
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P00883
ChainResidueDetails
AARG39
GARG39
GSER266
GARG298
ASER266
AARG298
BARG39
BSER266
BARG298
FARG39
FSER266
FARG298

site_idSWS_FT_FI4
Number of Residues4
DetailsSITE: Necessary for preference for fructose 1,6-bisphosphate over fructose 1-phosphate => ECO:0000250|UniProtKB:P00883
ChainResidueDetails
ATYR358
BTYR358
FTYR358
GTYR358

site_idSWS_FT_FI5
Number of Residues4
DetailsMOD_RES: N-acetylserine => ECO:0000250|UniProtKB:Q9LF98
ChainResidueDetails
ASER2
BSER2
FSER2
GSER2

site_idSWS_FT_FI6
Number of Residues4
DetailsMOD_RES: S-glutathionyl cysteine; transient => ECO:0000269|PubMed:21782461
ChainResidueDetails
ACYS68
BCYS68
FCYS68
GCYS68

site_idSWS_FT_FI7
Number of Residues4
DetailsMOD_RES: S-nitrosocysteine; transient; alternate => ECO:0000269|PubMed:21782461
ChainResidueDetails
ACYS173
BCYS173
FCYS173
GCYS173

site_idSWS_FT_FI8
Number of Residues4
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q9LF98
ChainResidueDetails
ASER350
BSER350
FSER350
GSER350

site_idSWS_FT_FI9
Number of Residues4
DetailsMOD_RES: N6,N6,N6-trimethyllysine => ECO:0000250|UniProtKB:Q9SJU4
ChainResidueDetails
ALYS354
BLYS354
FLYS354
GLYS354

237735

PDB entries from 2025-06-18

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