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4ZN3

Crystal Structure of MjSpt4:Spt5 complex conformation B

Functional Information from GO Data
ChainGOidnamespacecontents
A0003735molecular_functionstructural constituent of ribosome
A0003746molecular_functiontranslation elongation factor activity
A0005515molecular_functionprotein binding
A0005840cellular_componentribosome
A0006354biological_processDNA-templated transcription elongation
A0006355biological_processregulation of DNA-templated transcription
A0006357biological_processregulation of transcription by RNA polymerase II
A0006412biological_processtranslation
A0006414biological_processtranslational elongation
A0032784biological_processregulation of DNA-templated transcription elongation
A0140673biological_processtranscription elongation-coupled chromatin remodeling
B0005515molecular_functionprotein binding
B0006355biological_processregulation of DNA-templated transcription
B0008270molecular_functionzinc ion binding
B0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues2
Detailsbinding site for residue GOL A 201
ChainResidue
ALYS13
BLYS52

site_idAC2
Number of Residues6
Detailsbinding site for residue GOL A 202
ChainResidue
AGLU24
AHOH314
BVAL33
BLYS50
BGLY51
BLYS52

site_idAC3
Number of Residues5
Detailsbinding site for residue FE A 203
ChainResidue
AHIS145
BHIS-5
BHIS-3
BHOH204
AGLU90

site_idAC4
Number of Residues4
Detailsbinding site for residue FE A 204
ChainResidue
AASP147
BHIS-4
BHIS-6
BASP48

site_idAC5
Number of Residues4
Detailsbinding site for residue ZN B 101
ChainResidue
BCYS4
BCYS7
BCYS16
BCYS19

Functional Information from PROSITE/UniProt
site_idPS01108
Number of Residues18
DetailsRIBOSOMAL_L24 Ribosomal protein L24 signature. GDvVeIIaGpfKGer.AkV
ChainResidueDetails
AGLY92-VAL109

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00949, ECO:0000269|PubMed:20197319
ChainResidueDetails
BCYS4
BCYS7
BCYS16
BCYS19

222926

PDB entries from 2024-07-24

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