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6CFT

Structure of Human alpha-Phosphomannomutase 1 containing mutations R180T and R183I

Functional Information from GO Data
ChainGOidnamespacecontents
A0004615molecular_functionphosphomannomutase activity
A0005515molecular_functionprotein binding
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006013biological_processmannose metabolic process
A0006487biological_processprotein N-linked glycosylation
A0009298biological_processGDP-mannose biosynthetic process
A0016853molecular_functionisomerase activity
A0043025cellular_componentneuronal cell body
A0046872molecular_functionmetal ion binding
A1990830biological_processcellular response to leukemia inhibitory factor
Functional Information from PDB Data
site_idAC1
Number of Residues5
Detailsbinding site for residue MG A 301
ChainResidue
AASP19
AASP21
AASN218
AHOH404
AHOH430

site_idAC2
Number of Residues5
Detailsbinding site for residue MG A 302
ChainResidue
ATHR235
AGLU168
APHE230
AALA231
AASP232

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Nucleophile => ECO:0000269|PubMed:16540464
ChainResidueDetails
AASP19

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: Proton donor/acceptor => ECO:0000269|PubMed:16540464
ChainResidueDetails
AASP21

site_idSWS_FT_FI3
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:16540464, ECO:0007744|PDB:2FUC, ECO:0007744|PDB:2FUE
ChainResidueDetails
AASP19
AASP21
AASN218
APHE230
AASP232
ATHR235

site_idSWS_FT_FI4
Number of Residues7
DetailsBINDING: BINDING => ECO:0000269|PubMed:16540464
ChainResidueDetails
AARG28
AARG132
AARG143
AARG150
AMET186
ASER188
AASP190

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: N-acetylalanine => ECO:0007744|PubMed:22814378
ChainResidueDetails
AALA2

site_idSWS_FT_FI6
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:O35621
ChainResidueDetails
ASER242

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PDB entries from 2024-10-30

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