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2IEG

Crystal structure of rabbit muscle glycogen phosphorylase in complex with 3,4-dihydro-2-quinolone

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0004645molecular_function1,4-alpha-oligoglucan phosphorylase activity
A0005737cellular_componentcytoplasm
A0005975biological_processcarbohydrate metabolic process
A0005977biological_processglycogen metabolic process
A0005980biological_processglycogen catabolic process
A0008184molecular_functionglycogen phosphorylase activity
A0016757molecular_functionglycosyltransferase activity
A0030170molecular_functionpyridoxal phosphate binding
A0098723cellular_componentskeletal muscle myofibril
A0102250molecular_functionlinear malto-oligosaccharide phosphorylase activity
A0102499molecular_functionSHG alpha-glucan phosphorylase activity
B0000166molecular_functionnucleotide binding
B0004645molecular_function1,4-alpha-oligoglucan phosphorylase activity
B0005737cellular_componentcytoplasm
B0005975biological_processcarbohydrate metabolic process
B0005977biological_processglycogen metabolic process
B0005980biological_processglycogen catabolic process
B0008184molecular_functionglycogen phosphorylase activity
B0016757molecular_functionglycosyltransferase activity
B0030170molecular_functionpyridoxal phosphate binding
B0098723cellular_componentskeletal muscle myofibril
B0102250molecular_functionlinear malto-oligosaccharide phosphorylase activity
B0102499molecular_functionSHG alpha-glucan phosphorylase activity
Functional Information from PDB Data
site_idAC1
Number of Residues16
DetailsBINDING SITE FOR RESIDUE PLR A 903
ChainResidue
AGLY134
ALYS680
AHOH925
AHOH936
AHOH951
AHOH959
AHOH988
AHOH1266
ALYS568
ALYS574
ATYR648
AARG649
AVAL650
AGLY675
ATHR676
AGLY677

site_idAC2
Number of Residues17
DetailsBINDING SITE FOR RESIDUE PLR B 904
ChainResidue
BGLY134
BTRP491
BLYS568
BLYS574
BTYR648
BARG649
BVAL650
BGLY675
BTHR676
BGLY677
BLYS680
BHOH908
BHOH936
BHOH961
BHOH997
BHOH1007
BHOH1058

site_idAC3
Number of Residues14
DetailsBINDING SITE FOR RESIDUE FRY A 901
ChainResidue
AARG60
ATRP67
APRO188
AGLU190
ALYS191
AALA192
AHOH1104
AHOH1179
BTHR38
BLEU39
BVAL40
BHIS57
BTYR185
BGLY186

site_idAC4
Number of Residues15
DetailsBINDING SITE FOR RESIDUE FRY B 902
ChainResidue
ATHR38
ALEU39
AVAL40
APHE53
AHIS57
ATYR185
AGLY186
BARG60
BPRO188
BGLU190
BLYS191
BALA192
BHOH1107
BHOH1126
BHOH1230

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 Residues4
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P11217
ChainResidueDetails
AARG43
AARG310
BARG43
BARG310

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:3616621
ChainResidueDetails
AGLU76
BGLU76

site_idSWS_FT_FI3
Number of Residues4
DetailsSITE: Involved in the association of subunits => ECO:0000303|PubMed:728424
ChainResidueDetails
AASP109
APHE143
BASP109
BPHE143

site_idSWS_FT_FI4
Number of Residues2
DetailsSITE: Can be labeled by an AMP analog; may be involved in allosteric regulation => ECO:0000303|PubMed:728424
ChainResidueDetails
AGLY156
BGLY156

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: N-acetylserine => ECO:0000269|PubMed:3015680
ChainResidueDetails
AARG2
BARG2

site_idSWS_FT_FI6
Number of Residues2
DetailsMOD_RES: Phosphoserine; by PHK; in form phosphorylase A => ECO:0000250|UniProtKB:P11217
ChainResidueDetails
AVAL15
BVAL15

site_idSWS_FT_FI7
Number of Residues4
DetailsMOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:P09812
ChainResidueDetails
AGLY204
AASP227
BGLY204
BASP227

site_idSWS_FT_FI8
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q9WUB3
ChainResidueDetails
ALEU430
BLEU430

site_idSWS_FT_FI9
Number of Residues2
DetailsMOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:Q9WUB3
ChainResidueDetails
AGLU473
BGLU473

site_idSWS_FT_FI10
Number of Residues6
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P09812
ChainResidueDetails
AASP514
ASER747
AGLY748
BASP514
BSER747
BGLY748

site_idSWS_FT_FI11
Number of Residues2
DetailsMOD_RES: N6-(pyridoxal phosphate)lysine => ECO:0000269|PubMed:7500360, ECO:0000269|PubMed:8976550, ECO:0007744|PDB:2PRI, ECO:0007744|PDB:2SKC, ECO:0007744|PDB:2SKD, ECO:0007744|PDB:2SKE
ChainResidueDetails
APHE681
BPHE681

Catalytic Information from CSA
site_idCSA1
Number of Residues4
DetailsAnnotated By Reference To The Literature 1gpa
ChainResidueDetails
AARG569
ALYS568
ATHR676
ALYS574

site_idCSA2
Number of Residues4
DetailsAnnotated By Reference To The Literature 1gpa
ChainResidueDetails
BARG569
BLYS568
BTHR676
BLYS574

site_idMCSA1
Number of Residues6
DetailsM-CSA 205
ChainResidueDetails
ATHR378electrostatic stabiliser
AARG569electrostatic stabiliser
AILE570electrostatic stabiliser
AARG575electrostatic stabiliser
AGLY677electrostatic stabiliser
APHE681covalently attached

site_idMCSA2
Number of Residues6
DetailsM-CSA 205
ChainResidueDetails
BTHR378electrostatic stabiliser
BARG569electrostatic stabiliser
BILE570electrostatic stabiliser
BARG575electrostatic stabiliser
BGLY677electrostatic stabiliser
BPHE681covalently attached

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PDB entries from 2024-09-18

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