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1TRQ

X-RAY CRYSTALLOGRAPHIC AND CALORIMERIC STUDIES OF THE EFFECTS OF THE MUTATION TRP 59 TYR IN RIBONUCLEASE T1

Functional Information from GO Data
ChainGOidnamespacecontents
A0001411cellular_componenthyphal tip
A0003723molecular_functionRNA binding
A0004519molecular_functionendonuclease activity
A0004540molecular_functionRNA nuclease activity
A0008150biological_processbiological_process
A0016829molecular_functionlyase activity
A0030428cellular_componentcell septum
A0046589molecular_functionribonuclease T1 activity
B0001411cellular_componenthyphal tip
B0003723molecular_functionRNA binding
B0004519molecular_functionendonuclease activity
B0004540molecular_functionRNA nuclease activity
B0008150biological_processbiological_process
B0016829molecular_functionlyase activity
B0030428cellular_componentcell septum
B0046589molecular_functionribonuclease T1 activity
Functional Information from PDB Data
site_idAC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CA A 106
ChainResidue
AASP15
AHOH468
AHOH499

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA B 306
ChainResidue
BASP215
BHOH414
BHOH444
BHOH456
BHOH479

site_idAC3
Number of Residues13
DetailsBINDING SITE FOR RESIDUE 2GP A 105
ChainResidue
AHIS40
ALYS41
ATYR42
AASN43
AASN44
ATYR45
AGLU46
AGLU58
AARG77
AHIS92
AASN98
APHE100
ATYR38

site_idAC4
Number of Residues13
DetailsBINDING SITE FOR RESIDUE 2GP B 305
ChainResidue
BTYR238
BHIS240
BTYR242
BASN243
BASN244
BTYR245
BGLU246
BGLU258
BARG277
BHIS292
BASN298
BASN299
BPHE300

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: ACT_SITE => ECO:0000269|PubMed:2844811
ChainResidueDetails
AHIS40
BHIS240

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000269|PubMed:2844811
ChainResidueDetails
AGLU58
BGLU258

site_idSWS_FT_FI3
Number of Residues2
DetailsACT_SITE: Proton donor
ChainResidueDetails
AHIS92
BHIS292

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

site_idCSA2
Number of Residues3
DetailsAnnotated By Reference To The Literature 1b2m
ChainResidueDetails
BHIS292
BGLU258
BHIS240

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

site_idMCSA2
Number of Residues6
DetailsM-CSA 414
ChainResidueDetails
BTYR238electrostatic stabiliser
BHIS240proton shuttle (general acid/base)
BGLU258proton shuttle (general acid/base)
BARG277electrostatic stabiliser
BHIS292proton shuttle (general acid/base)
BPHE300electrostatic stabiliser

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PDB entries from 2024-06-26

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