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1RLS

CRYSTAL STRUCTURE OF RNASE T1 COMPLEXED WITH THE PRODUCT NUCLEOTIDE 3'-GMP. STRUCTURAL EVIDENCE FOR DIRECT INTERACTION OF HISTIDINE 40 AND GLUTAMIC ACID 58 WITH THE 2'-HYDROXYL GROUP OF RIBOSE

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 Residues5
DetailsBINDING SITE FOR RESIDUE CA A 106
ChainResidue
AASP15
AHOH204
AHOH214
AHOH216
AHOH239

site_idAC2
Number of Residues14
DetailsBINDING SITE FOR RESIDUE 3GP A 105
ChainResidue
AASN43
AASN44
ATYR45
AGLU46
AGLU58
AARG77
AHIS92
AASN98
APHE100
AHOH278
ATYR38
AHIS40
ALYS41
ATYR42

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
AHIS92

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1b2m
ChainResidueDetails
AGLU58
AHIS40
AHIS92

site_idMCSA1
Number of Residues6
DetailsM-CSA 414
ChainResidueDetails
ATYR38electrostatic stabiliser
AHIS40proton shuttle (general acid/base)
AGLU58proton shuttle (general acid/base)
AARG77electrostatic stabiliser
AHIS92proton shuttle (general acid/base)
APHE100electrostatic stabiliser

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PDB entries from 2024-07-24

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