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1VKL

RABBIT MUSCLE PHOSPHOGLUCOMUTASE

Functional Information from GO Data
ChainGOidnamespacecontents
A0000287molecular_functionmagnesium ion binding
A0004614molecular_functionphosphoglucomutase activity
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0005975biological_processcarbohydrate metabolic process
A0006006biological_processglucose metabolic process
A0016529cellular_componentsarcoplasmic reticulum
A0016853molecular_functionisomerase activity
A0016868molecular_functionintramolecular phosphotransferase activity
A0046872molecular_functionmetal ion binding
B0000287molecular_functionmagnesium ion binding
B0004614molecular_functionphosphoglucomutase activity
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0005975biological_processcarbohydrate metabolic process
B0006006biological_processglucose metabolic process
B0016529cellular_componentsarcoplasmic reticulum
B0016853molecular_functionisomerase activity
B0016868molecular_functionintramolecular phosphotransferase activity
B0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE NI A 562
ChainResidue
AASP287
AASP289
AASP291
ASEP116

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE NI B 562
ChainResidue
BSEP116
BASP287
BASP289
BASP291
BHOH706

site_idMBA
Number of Residues4
DetailsMETAL ATOM IN 562.
ChainResidue
AASP287
AASP289
AASP291
ASEP116

site_idMBB
Number of Residues4
DetailsMETAL ATOM IN 562.
ChainResidue
BASP287
BASP289
BASP291
BSEP116

Functional Information from PROSITE/UniProt
site_idPS00710
Number of Residues10
DetailsPGM_PMM Phosphoglucomutase and phosphomannomutase phosphoserine signature. GIiLTASHNP
ChainResidueDetails
AGLY110-PRO119

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsActive site: {"description":"Phosphoserine intermediate","evidences":[{"source":"PubMed","id":"5669853","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues12
DetailsBinding site: {"evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"AUG-1999","submissionDatabase":"PDB data bank","title":"Binding driven structural changes in crystaline phosphoglucomutase associated with chemical reaction.","authors":["Baranidharan S.","Ray W.J. Jr.","Liu Y."]}},{"source":"PDB","id":"1C47","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues2
DetailsBinding site: {"description":"via phosphate group","evidences":[{"source":"PubMed","id":"15299905","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3PMG","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues6
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"15299905","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3PMG","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues2
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P36871","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues4
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"Q9D0F9","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"15299905","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3PMG","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues10
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P38652","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues2
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"P36871","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues2
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"Q9D0F9","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI11
Number of Residues2
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"Q9D0F9","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI12
Number of Residues6
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P36871","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI13
Number of Residues2
DetailsModified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"Q9D0F9","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI14
Number of Residues2
DetailsModified residue: {"description":"Phosphothreonine; by PAK1","evidences":[{"source":"UniProtKB","id":"P36871","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idMCSA1
Number of Residues7
DetailsM-CSA 352
ChainResidueDetails
ASEP116activator, covalently attached, metal ligand, nucleofuge, nucleophile, proton acceptor, proton donor
AGLY121proton acceptor, proton donor
AASP291metal ligand
AASN293metal ligand
AILE295metal ligand
ALEU296electrostatic stabiliser
ATRP392proton acceptor, proton donor

site_idMCSA2
Number of Residues7
DetailsM-CSA 352
ChainResidueDetails
BSEP116activator, covalently attached, metal ligand, nucleofuge, nucleophile, proton acceptor, proton donor
BGLY121proton acceptor, proton donor
BASP291metal ligand
BASN293metal ligand
BILE295metal ligand
BLEU296electrostatic stabiliser
BTRP392proton acceptor, proton donor

239492

PDB entries from 2025-07-30

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