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7O58

Human phosphomannomutase 2 (PMM2) with mutation T237M in complex with the activator glucose 1,6-bisphosphate

Functional Information from GO Data
ChainGOidnamespacecontents
A0004615molecular_functionphosphomannomutase activity
A0005515molecular_functionprotein binding
A0005654cellular_componentnucleoplasm
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006013biological_processmannose metabolic process
A0006486biological_processprotein glycosylation
A0006487biological_processprotein N-linked glycosylation
A0009298biological_processGDP-mannose biosynthetic process
A0016853molecular_functionisomerase activity
A0019309biological_processmannose catabolic process
A0043025cellular_componentneuronal cell body
A0046872molecular_functionmetal ion binding
A0061728biological_processGDP-mannose biosynthetic process from mannose
A0061729biological_processGDP-mannose biosynthetic process from fructose-6-phosphate
B0004615molecular_functionphosphomannomutase activity
B0005515molecular_functionprotein binding
B0005654cellular_componentnucleoplasm
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0006013biological_processmannose metabolic process
B0006486biological_processprotein glycosylation
B0006487biological_processprotein N-linked glycosylation
B0009298biological_processGDP-mannose biosynthetic process
B0016853molecular_functionisomerase activity
B0019309biological_processmannose catabolic process
B0043025cellular_componentneuronal cell body
B0046872molecular_functionmetal ion binding
B0061728biological_processGDP-mannose biosynthetic process from mannose
B0061729biological_processGDP-mannose biosynthetic process from fructose-6-phosphate
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Nucleophile => ECO:0000250|UniProtKB:Q92871
ChainResidueDetails
AASP12
BASP12

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Proton donor/acceptor => ECO:0000250|UniProtKB:Q92871
ChainResidueDetails
AASP14
BASP14

site_idSWS_FT_FI3
Number of Residues22
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:Q92871
ChainResidueDetails
AASP12
AASP223
ATHR226
BASP12
BASP14
BARG21
BARG123
BARG134
BARG141
BSER179
BASP181
AASP14
BPHE221
BASP223
BTHR226
AARG21
AARG123
AARG134
AARG141
ASER179
AASP181
APHE221

site_idSWS_FT_FI4
Number of Residues2
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P31353
ChainResidueDetails
AASP209
BASP209

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: N-acetylalanine => ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378
ChainResidueDetails
AALA2
BALA2

site_idSWS_FT_FI6
Number of Residues2
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:Q9Z2M7
ChainResidueDetails
ALYS149
BLYS149

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PDB entries from 2024-07-24

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