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4XC5

CRYSTAL STRUCTURE OF THE T1L REOVIRUS ATTACHMENT PROTEIN SIGMA1

Functional Information from GO Data
ChainGOidnamespacecontents
A0003700molecular_functionDNA-binding transcription factor activity
A0006355biological_processregulation of DNA-templated transcription
A0007155biological_processcell adhesion
A0019058biological_processviral life cycle
A0019062biological_processvirion attachment to host cell
B0003700molecular_functionDNA-binding transcription factor activity
B0006355biological_processregulation of DNA-templated transcription
B0007155biological_processcell adhesion
B0019058biological_processviral life cycle
B0019062biological_processvirion attachment to host cell
C0003700molecular_functionDNA-binding transcription factor activity
C0006355biological_processregulation of DNA-templated transcription
C0007155biological_processcell adhesion
C0019058biological_processviral life cycle
C0019062biological_processvirion attachment to host cell
Functional Information from PDB Data
site_idAC1
Number of Residues2
Detailsbinding site for residue CL A 501
ChainResidue
AGLY398
BASN321

site_idAC2
Number of Residues6
Detailsbinding site for residue MG A 502
ChainResidue
AASN375
AASN375
ASER376
ASER376
ATHR454
ATHR454

site_idAC3
Number of Residues4
Detailsbinding site for residue ACT A 503
ChainResidue
BVAL326
BALA327
BGLY331
AASP363

site_idAC4
Number of Residues5
Detailsbinding site for residue GOL A 504
ChainResidue
AVAL354
ATHR355
ASER370
AGLN371
AMET372

site_idAC5
Number of Residues3
Detailsbinding site for residue GOL A 505
ChainResidue
AASP426
CTHR449
CTYR450

site_idAC6
Number of Residues2
Detailsbinding site for residue CL B 501
ChainResidue
BGLY398
CASN321

site_idAC7
Number of Residues6
Detailsbinding site for residue MG B 502
ChainResidue
BASN375
BASN375
BSER376
BSER376
BTHR454
BTHR454

site_idAC8
Number of Residues4
Detailsbinding site for residue ACT B 503
ChainResidue
BASP363
CVAL326
CALA327
CGLY331

site_idAC9
Number of Residues6
Detailsbinding site for residue GOL B 504
ChainResidue
BVAL354
BTHR355
BSER370
BGLN371
BMET372
BHOH606

site_idAD1
Number of Residues5
Detailsbinding site for residue GOL B 505
ChainResidue
BTHR449
BTYR450
CARG424
CILE425
CASP426

site_idAD2
Number of Residues3
Detailsbinding site for residue GOL B 506
ChainResidue
ATHR449
ATYR450
BASP426

site_idAD3
Number of Residues2
Detailsbinding site for residue CL C 501
ChainResidue
AASN321
CGLY398

site_idAD4
Number of Residues6
Detailsbinding site for residue MG C 502
ChainResidue
CASN375
CASN375
CSER376
CSER376
CTHR454
CTHR454

site_idAD5
Number of Residues3
Detailsbinding site for residue ACT C 503
ChainResidue
AALA327
AGLY331
CASP363

site_idAD6
Number of Residues6
Detailsbinding site for residue GOL C 504
ChainResidue
AALA320
AASN321
CVAL388
CGLN396
CTHR397
CHOH604

site_idAD7
Number of Residues5
Detailsbinding site for residue GOL C 505
ChainResidue
CVAL354
CTHR355
CSER370
CGLN371
CMET372

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues51
DetailsRegion: {"description":"Binding to GM2 ganglioside","evidences":[{"source":"PubMed","id":"23236285","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues3
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine; by host","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

248636

PDB entries from 2026-02-04

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