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6OH4

X-ray crystal structure of the mouse CMP-sialic acid transporter in complex with CMP, by hanging drop vapor diffusion

Functional Information from GO Data
ChainGOidnamespacecontents
A0000139cellular_componentGolgi membrane
A0005456molecular_functionCMP-N-acetylneuraminate transmembrane transporter activity
A0005794cellular_componentGolgi apparatus
A0015165molecular_functionpyrimidine nucleotide-sugar transmembrane transporter activity
A0015297molecular_functionantiporter activity
A0015782biological_processCMP-N-acetylneuraminate transmembrane transport
A0016020cellular_componentmembrane
A0071702biological_processobsolete organic substance transport
A0090481biological_processpyrimidine nucleotide-sugar transmembrane transport
B0000139cellular_componentGolgi membrane
B0005456molecular_functionCMP-N-acetylneuraminate transmembrane transporter activity
B0005794cellular_componentGolgi apparatus
B0015165molecular_functionpyrimidine nucleotide-sugar transmembrane transporter activity
B0015297molecular_functionantiporter activity
B0015782biological_processCMP-N-acetylneuraminate transmembrane transport
B0016020cellular_componentmembrane
B0071702biological_processobsolete organic substance transport
B0090481biological_processpyrimidine nucleotide-sugar transmembrane transport
Functional Information from PDB Data
site_idAC1
Number of Residues13
Detailsbinding site for residue C5P A 401
ChainResidue
ALYS55
ATYR214
AGLY257
ASER261
ALYS272
ATYR98
AGLN101
AASN102
ATYR121
ALYS124
ASER188
APHE195
AASN210

site_idAC2
Number of Residues14
Detailsbinding site for residue C5P B 401
ChainResidue
BLYS55
BTYR98
BGLN101
BASN102
BTYR121
BLYS124
BSER188
BPHE195
BASN210
BMET213
BTYR214
BGLY257
BSER261
BLYS272

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues56
DetailsTOPO_DOM: Cytoplasmic => ECO:0000269|PubMed:10085119, ECO:0000269|PubMed:30985278
ChainResidueDetails
AMET1-SER9
APRO316-VAL336
BMET1-SER9
BPRO316-VAL336

site_idSWS_FT_FI2
Number of Residues376
DetailsTRANSMEM: Helical => ECO:0000269|PubMed:30985278
ChainResidueDetails
ALEU10-ALA30
ALEU297-LEU315
BLEU10-ALA30
BTHR46-ALA64
BLEU88-ALA108
BALA115-MET135
BLYS142-TRP160
BLEU176-GLU196
BASN210-SER228
BTYR244-VAL262
BILE270-VAL288
ATHR46-ALA64
BLEU297-LEU315
ALEU88-ALA108
AALA115-MET135
ALYS142-TRP160
ALEU176-GLU196
AASN210-SER228
ATYR244-VAL262
AILE270-VAL288

site_idSWS_FT_FI3
Number of Residues108
DetailsTOPO_DOM: Lumenal => ECO:0000269|PubMed:30985278
ChainResidueDetails
ALEU31-THR45
BLEU289-THR296
ALEU109-ALA114
ALYS161-LEU175
AASP229-THR243
ALEU289-THR296
BLEU31-THR45
BLEU109-ALA114
BLYS161-LEU175
BASP229-THR243

site_idSWS_FT_FI4
Number of Residues90
DetailsTOPO_DOM: Cytoplasmic => ECO:0000269|PubMed:30985278
ChainResidueDetails
ALYS65-GLU87
ALEU136-SER141
ALYS197-ARG209
AVAL263-ASN269
BLYS65-GLU87
BLEU136-SER141
BLYS197-ARG209
BVAL263-ASN269

site_idSWS_FT_FI5
Number of Residues12
DetailsBINDING: BINDING => ECO:0000269|PubMed:30985278, ECO:0007744|PDB:6OH2, ECO:0007744|PDB:6OH3
ChainResidueDetails
ALYS55
BSER188
BASN210
BLYS272
AGLN101
ATYR117
ASER188
AASN210
ALYS272
BLYS55
BGLN101
BTYR117

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PDB entries from 2024-06-19

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