Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

4HE2

Crystal structure of human muscle fructose-1,6-bisphosphatase Q32R mutant complex with AMP

Functional Information from GO Data
ChainGOidnamespacecontents
A0005515molecular_functionprotein binding
A0005634cellular_componentnucleus
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0005886cellular_componentplasma membrane
A0005975biological_processcarbohydrate metabolic process
A0005986biological_processsucrose biosynthetic process
A0006000biological_processfructose metabolic process
A0006002biological_processfructose 6-phosphate metabolic process
A0006094biological_processgluconeogenesis
A0016787molecular_functionhydrolase activity
A0016791molecular_functionphosphatase activity
A0030018cellular_componentZ disc
A0030388biological_processfructose 1,6-bisphosphate metabolic process
A0042132molecular_functionfructose 1,6-bisphosphate 1-phosphatase activity
A0042578molecular_functionphosphoric ester hydrolase activity
A0042802molecular_functionidentical protein binding
A0046872molecular_functionmetal ion binding
A0070062cellular_componentextracellular exosome
A0070161cellular_componentanchoring junction
Functional Information from PDB Data
site_idAC1
Number of Residues19
DetailsBINDING SITE FOR RESIDUE AMP A 401
ChainResidue
AVAL17
ALYS112
ATYR113
AVAL160
ATHR177
AHOH535
AHOH594
AHOH605
AHOH612
AHOH663
AHOH746
ALYS20
AGLY21
AALA24
ATHR27
AGLY28
AGLU29
ALEU30
ATHR31

site_idAC2
Number of Residues16
DetailsBINDING SITE FOR RESIDUE PO3 A 402
ChainResidue
AGLU97
AASP118
ALEU120
AASP121
AGLY122
ASER123
AGLU280
AMG403
AZN404
AMG405
AMG406
AHOH561
AHOH628
AHOH648
AHOH740
AHOH757

site_idAC3
Number of Residues8
DetailsBINDING SITE FOR RESIDUE MG A 403
ChainResidue
AGLU97
AASP118
AASP121
AGLU280
APO3402
AZN404
AMG405
AHOH740

site_idAC4
Number of Residues7
DetailsBINDING SITE FOR RESIDUE ZN A 404
ChainResidue
AGLU97
AASP118
AASP121
AGLU280
APO3402
AMG403
AMG405

site_idAC5
Number of Residues9
DetailsBINDING SITE FOR RESIDUE MG A 405
ChainResidue
AGLU97
AASP118
ALEU120
APO3402
AMG403
AZN404
AMG406
AHOH524
AHOH561

site_idAC6
Number of Residues7
DetailsBINDING SITE FOR RESIDUE MG A 406
ChainResidue
AGLU97
APO3402
AMG405
AHOH561
AHOH600
AHOH628
AHOH757

site_idAC7
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CL A 407
ChainResidue
ASER131
ASER131

Functional Information from PROSITE/UniProt
site_idPS00124
Number of Residues13
DetailsFBPASE Fructose-1-6-bisphosphatase active site. GKLrlLYEcnPVA
ChainResidueDetails
AGLY273-ALA285

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:22120740
ChainResidueDetails
AVAL17
ATHR27
ALYS112
AARG140

site_idSWS_FT_FI2
Number of Residues10
DetailsBINDING:
ChainResidueDetails
AASP68
AGLU280
AGLU97
AASP118
ALEU120
AASP121
AASN212
ATYR244
ATYR264
ALYS274

site_idSWS_FT_FI3
Number of Residues1
DetailsSITE: Important for the conversion from active R-state to inactive T-state in the presence of AMP
ChainResidueDetails
AARG32

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:Q9Z1N1
ChainResidueDetails
ATYR215
ATYR218

226707

PDB entries from 2024-10-30

PDB statisticsPDBj update infoContact PDBjnumon