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1FA9

HUMAN LIVER GLYCOGEN PHOSPHORYLASE A COMPLEXED WITH AMP

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0002060molecular_functionpurine nucleobase binding
A0003824molecular_functioncatalytic activity
A0004645molecular_function1,4-alpha-oligoglucan phosphorylase activity
A0005515molecular_functionprotein binding
A0005524molecular_functionATP binding
A0005536molecular_functionglucose binding
A0005576cellular_componentextracellular region
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0005975biological_processcarbohydrate metabolic process
A0005977biological_processglycogen metabolic process
A0005980biological_processglycogen catabolic process
A0006015biological_process5-phosphoribose 1-diphosphate biosynthetic process
A0008152biological_processmetabolic process
A0008184molecular_functionglycogen phosphorylase activity
A0009617biological_processresponse to bacterium
A0016208molecular_functionAMP binding
A0016740molecular_functiontransferase activity
A0016757molecular_functionglycosyltransferase activity
A0019842molecular_functionvitamin binding
A0030170molecular_functionpyridoxal phosphate binding
A0030246molecular_functioncarbohydrate binding
A0032052molecular_functionbile acid binding
A0034774cellular_componentsecretory granule lumen
A0042593biological_processglucose homeostasis
A0042802molecular_functionidentical protein binding
A0070062cellular_componentextracellular exosome
A0070266biological_processnecroptotic process
A0102250molecular_functionlinear malto-oligosaccharide phosphorylase activity
A0102499molecular_functionSHG alpha-glucan phosphorylase activity
A1904813cellular_componentficolin-1-rich granule lumen
Functional Information from PROSITE/UniProt
site_idPS00102
Number of Residues13
DetailsPHOSPHORYLASE Phosphorylase pyridoxal-phosphate attachment site. EASGtGnMKfmLN
ChainResidueDetails
AGLU672-ASN684

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsBINDING: BINDING => ECO:0000269|PubMed:10949035, ECO:0007744|PDB:1FA9
ChainResidueDetails
AASP42
ATYR75
AARG309

site_idSWS_FT_FI2
Number of Residues2
DetailsSITE: Involved in the association of subunits => ECO:0000250|UniProtKB:P00489
ChainResidueDetails
ACYS108
ACYS142

site_idSWS_FT_FI3
Number of Residues1
DetailsSITE: May be involved in allosteric control => ECO:0000250|UniProtKB:P00489
ChainResidueDetails
ATYR155

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: N-acetylalanine => ECO:0007744|PubMed:19413330
ChainResidueDetails
AALA1

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: Phosphoserine; by PHK; in form phosphorylase a => ECO:0000269|PubMed:10949035, ECO:0000269|PubMed:22225877, ECO:0007744|PDB:1FA9
ChainResidueDetails
ASEP14

site_idSWS_FT_FI6
Number of Residues1
DetailsMOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:Q9ET01
ChainResidueDetails
ALYS363

site_idSWS_FT_FI7
Number of Residues2
DetailsMOD_RES: N6-acetyllysine => ECO:0000269|PubMed:22225877
ChainResidueDetails
ALYS469
ALYS795

site_idSWS_FT_FI8
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q9ET01
ChainResidueDetails
ASER523

site_idSWS_FT_FI9
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P09811
ChainResidueDetails
ASER560

site_idSWS_FT_FI10
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:24275569
ChainResidueDetails
ASER638

site_idSWS_FT_FI11
Number of Residues1
DetailsMOD_RES: N6-(pyridoxal phosphate)lysine => ECO:0000269|PubMed:10949035, ECO:0000269|PubMed:10980448, ECO:0000269|PubMed:12204691, ECO:0007744|PDB:1EM6, ECO:0007744|PDB:1EXV, ECO:0007744|PDB:1FA9, ECO:0007744|PDB:1FC0, ECO:0007744|PDB:1L5Q, ECO:0007744|PDB:1L5R, ECO:0007744|PDB:1L5S, ECO:0007744|PDB:1L7X
ChainResidueDetails
ALYS680

218853

PDB entries from 2024-04-24

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