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3BIR

DISECTING HISTIDINE INTERACTIONS IN RIBONUCLEASE T1 BY ASN AND GLN SUBSTITUTIONS

Functional Information from GO Data
ChainGOidnamespacecontents
A0001411cellular_componenthyphal tip
A0003723molecular_functionRNA binding
A0004519molecular_functionendonuclease activity
A0004521molecular_functionRNA endonuclease activity
A0004540molecular_functionRNA nuclease activity
A0008150biological_processbiological_process
A0016829molecular_functionlyase activity
A0030428cellular_componentcell septum
A0046589molecular_functionribonuclease T1 activity
Functional Information from PDB Data
site_idAC1
Number of Residues7
DetailsBINDING SITE FOR RESIDUE CA A 106
ChainResidue
AHOH219
AHOH238
AHOH241
AASP15
AHOH206
AHOH212
AHOH214

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 107
ChainResidue
AASP49
AASN98
A2GP105
AHOH217
AHOH221
AHOH260

site_idAC3
Number of Residues15
DetailsBINDING SITE FOR RESIDUE 2GP A 105
ChainResidue
AASN36
ATYR38
AHIS40
ALYS41
ATYR42
AASN43
AASN44
ATYR45
AGLU46
AGLU58
AASN98
APHE100
ACA107
AHOH217
AHOH260

site_idCAT
Number of Residues5
DetailsCATALYTIC SITE.
ChainResidue
AASN92
AGLU58
AHIS40
ATYR38
APHE100

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: ACT_SITE => ECO:0000269|PubMed:2844811
ChainResidueDetails
AHIS40

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: Proton acceptor => ECO:0000269|PubMed:2844811
ChainResidueDetails
AGLU58

site_idSWS_FT_FI3
Number of Residues1
DetailsACT_SITE: Proton donor
ChainResidueDetails
AASN92

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1b2m
ChainResidueDetails
AGLU58
AHIS40
AASN92

site_idMCSA1
Number of Residues6
DetailsM-CSA 414
ChainResidueDetails
ATYR38electrostatic stabiliser
AHIS40proton shuttle (general acid/base)
AGLU58proton shuttle (general acid/base)
AARG77electrostatic stabiliser
AASN92proton shuttle (general acid/base)
APHE100electrostatic stabiliser

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PDB entries from 2024-11-06

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