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2AAE

THE ROLE OF HISTIDINE-40 IN RIBONUCLEASE T1 CATALYSIS: THREE-DIMENSIONAL STRUCTURES OF THE PARTIALLY ACTIVE HIS40LYS MUTANT

Functional Information from GO Data
ChainGOidnamespacecontents
A0001411cellular_componenthyphal tip
A0003723molecular_functionRNA binding
A0004518molecular_functionnuclease activity
A0004519molecular_functionendonuclease activity
A0004540molecular_functionRNA nuclease activity
A0008150biological_processbiological_process
A0016787molecular_functionhydrolase activity
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 105
ChainResidue
AHOH161
AHOH178
AHOH188
AHOH189
AASP15
AHOH141
AHOH156

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE PO4 A 106
ChainResidue
ATYR38
ALYS40
AGLU58
AARG77
AHIS92
APHE100

site_idCAL
Number of Residues1
Details
ChainResidue
AASP15

site_idCAT
Number of Residues5
Details
ChainResidue
ATYR38
ALYS40
AGLU58
AARG77
AHIS92

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: ACT_SITE => ECO:0000269|PubMed:2844811
ChainResidueDetails
ALYS40

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_idMCSA1
Number of Residues6
DetailsM-CSA 414
ChainResidueDetails
ATYR38electrostatic stabiliser
ALYS40proton 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 2024-04-24

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