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5BIR

DISECTING HISTIDINE INTERACTIONS IN RIBONUCLEASE T1 USING ASN AND GLN MUTATIONS

Functional Information from GO Data
ChainGOidnamespacecontents
A0001411cellular_componenthyphal tip
A0003723molecular_functionRNA binding
A0004518molecular_functionnuclease activity
A0004519molecular_functionendonuclease activity
A0004521molecular_functionRNA endonuclease activity
A0004540molecular_functionRNA nuclease activity
A0016787molecular_functionhydrolase activity
A0016829molecular_functionlyase activity
A0030428cellular_componentcell septum
A0046589molecular_functionribonuclease T1 activity
B0001411cellular_componenthyphal tip
B0003723molecular_functionRNA binding
B0004518molecular_functionnuclease activity
B0004519molecular_functionendonuclease activity
B0004521molecular_functionRNA endonuclease activity
B0004540molecular_functionRNA nuclease activity
B0016787molecular_functionhydrolase activity
B0016829molecular_functionlyase activity
B0030428cellular_componentcell septum
B0046589molecular_functionribonuclease T1 activity
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA B 501
ChainResidue
BGLN85
BHOH626
AGLN92
AALA95
AHOH108
AHOH119

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA B 601
ChainResidue
BTYR45
BGLY47
BASP49
BHOH644
BHOH671

site_idAC3
Number of Residues15
DetailsBINDING SITE FOR RESIDUE 2GP A 105
ChainResidue
ATYR38
AHIS40
ALYS41
ATYR42
AASN43
AASN44
ATYR45
AGLU46
AGLU58
AARG77
AGLN92
AASN98
APHE100
AHOH132
BASN83

site_idAC4
Number of Residues11
DetailsBINDING SITE FOR RESIDUE 2GP B 306
ChainResidue
BTYR38
BHIS40
BLYS41
BTYR42
BASN43
BASN44
BTYR45
BGLU46
BGLU58
BASN98
BPHE100

site_idCAT
Number of Residues5
DetailsCATALYTIC SITE.
ChainResidue
AGLN92
AGLU58
AHIS40
ATYR38
APHE100

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsActive site: {"evidences":[{"source":"PubMed","id":"2844811","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues2
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"PubMed","id":"2844811","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues2
DetailsActive site: {"description":"Proton donor"}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1b2m
ChainResidueDetails
AGLU58
AHIS40
AGLN92

site_idCSA2
Number of Residues3
DetailsAnnotated By Reference To The Literature 1b2m
ChainResidueDetails
BGLU58
BHIS40
BGLN92

site_idMCSA1
Number of Residues6
DetailsM-CSA 414
ChainResidueDetails
ATYR38electrostatic stabiliser
AHIS40proton shuttle (general acid/base)
AGLU58proton shuttle (general acid/base)
AARG77electrostatic stabiliser
AGLN92proton shuttle (general acid/base)
APHE100electrostatic stabiliser

site_idMCSA2
Number of Residues6
DetailsM-CSA 414
ChainResidueDetails
BTYR38electrostatic stabiliser
BHIS40proton shuttle (general acid/base)
BGLU58proton shuttle (general acid/base)
BARG77electrostatic stabiliser
BGLN92proton shuttle (general acid/base)
BPHE100electrostatic stabiliser

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PDB entries from 2026-02-25

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