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1UMG

Crystal structure of fructose-1,6-bisphosphatase

Functional Information from GO Data
ChainGOidnamespacecontents
A0000287molecular_functionmagnesium ion binding
A0004332molecular_functionfructose-bisphosphate aldolase activity
A0006094biological_processgluconeogenesis
A0006096biological_processglycolytic process
A0006740biological_processNADPH regeneration
A0016311biological_processdephosphorylation
A0016787molecular_functionhydrolase activity
A0016829molecular_functionlyase activity
A0042132molecular_functionfructose 1,6-bisphosphate 1-phosphatase activity
A0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG A 401
ChainResidue
AASP233
A2FP400
AMG402
AHOH408
AHOH409
AHOH410

site_idAC2
Number of Residues8
DetailsBINDING SITE FOR RESIDUE MG A 402
ChainResidue
AMG401
AMG403
AHOH406
AHOH411
AHOH412
AASP233
AASP234
A2FP400

site_idAC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE MG A 403
ChainResidue
AASP53
AASP54
AASP132
AASP234
A2FP400
AMG402
AHOH406

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG A 404
ChainResidue
AASP12
AHIS19
AASP53
AGLN95
A2FP400
AHOH407

site_idAC5
Number of Residues31
DetailsBINDING SITE FOR RESIDUE 2FP A 400
ChainResidue
AASP12
AHIS19
AASP53
ATYR91
AGLN95
ASER103
AGLY104
AASN105
AASP132
ALYS133
AASP233
AASP234
AGLN242
AHIS243
AALA247
ATRP264
AMET265
AARG266
AGLY267
AASP287
ATYR348
AMG401
AMG402
AMG403
AMG404
AHOH406
AHOH408
AHOH409
AHOH410
AHOH457
AHOH472

site_idAC6
Number of Residues7
DetailsBINDING SITE FOR RESIDUE MPD A 405
ChainResidue
AASP317
AASP317
AARG320
AASN324
AHOH421
AHOH526
AHOH653

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton acceptor; for FBP phosphatase activity => ECO:0000305|PubMed:15274916, ECO:0000305|PubMed:21983966
ChainResidueDetails
AASP12

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: Proton donor/acceptor; for FBP aldolase activity => ECO:0000305|PubMed:21983966
ChainResidueDetails
ATYR229

site_idSWS_FT_FI3
Number of Residues1
DetailsACT_SITE: Schiff-base intermediate with DHAP; for FBP aldolase activity => ECO:0000269|PubMed:21983966
ChainResidueDetails
ALYS232

site_idSWS_FT_FI4
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:15274916, ECO:0000269|PubMed:21983966, ECO:0007744|PDB:1UMG, ECO:0007744|PDB:3R1M
ChainResidueDetails
AASP12
AHIS19
AASP53
AASP54
AGLN95
AASP132

site_idSWS_FT_FI5
Number of Residues3
DetailsBINDING: in other chain => ECO:0000269|PubMed:15274916, ECO:0007744|PDB:1UMG
ChainResidueDetails
ATYR91
AGLY104
ATYR348

site_idSWS_FT_FI6
Number of Residues3
DetailsBINDING: BINDING => ECO:0000269|PubMed:21983966, ECO:0007744|PDB:3R1M
ChainResidueDetails
ALYS133
AARG266
AASP287

site_idSWS_FT_FI7
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:21983966
ChainResidueDetails
ALYS232

site_idSWS_FT_FI8
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:15274916
ChainResidueDetails
AASP233

site_idSWS_FT_FI9
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:15274916, ECO:0000269|PubMed:21983966
ChainResidueDetails
AASP234

site_idSWS_FT_FI10
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:15274916, ECO:0007744|PDB:1UMG
ChainResidueDetails
AGLN242

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PDB entries from 2025-06-11

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