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2AAD

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
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 Residues6
DetailsBINDING SITE FOR RESIDUE CA A 106
ChainResidue
AASP15
AHOH136
AHOH142
AHOH143
AHOH177
AHOH181

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA B 107
ChainResidue
BASP15
BHOH122
BHOH137
BHOH216
BHOH217
BHOH218

site_idAC3
Number of Residues15
DetailsBINDING SITE FOR RESIDUE 2GP A 105
ChainResidue
ATYR38
ALYS40
ALYS41
ATYR42
AASN43
AASN44
ATYR45
AGLU46
AGLU58
AARG77
AHIS92
AASN98
APHE100
AHOH172
AHOH199

site_idAC4
Number of Residues16
DetailsBINDING SITE FOR RESIDUE 2GP B 105
ChainResidue
BTYR38
BLYS40
BLYS41
BTYR42
BASN43
BASN44
BTYR45
BGLU46
BGLU58
BARG77
BHIS92
BASN98
BASN99
BPHE100
BHOH139
BHOH142

site_idBIN
Number of Residues12
Details
ChainResidue
ATYR42
AASN43
AASN44
ATYR45
AGLU46
AASN98
BTYR42
BASN43
BASN44
BTYR45
BGLU46
BASN98

site_idCAL
Number of Residues2
Details
ChainResidue
AASP15
BASP15

site_idCAT
Number of Residues10
Details
ChainResidue
ATYR38
BHIS92
ALYS40
AGLU58
AARG77
AHIS92
BTYR38
BLYS40
BGLU58
BARG77

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: ACT_SITE => ECO:0000269|PubMed:2844811
ChainResidueDetails
ALYS40
BLYS40

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000269|PubMed:2844811
ChainResidueDetails
AGLU58
BGLU58

site_idSWS_FT_FI3
Number of Residues2
DetailsACT_SITE: Proton donor
ChainResidueDetails
AHIS92
BHIS92

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

site_idMCSA2
Number of Residues6
DetailsM-CSA 414
ChainResidueDetails
BTYR38electrostatic stabiliser
BLYS40proton shuttle (general acid/base)
BGLU58proton shuttle (general acid/base)
BARG77electrostatic stabiliser
BHIS92proton shuttle (general acid/base)
BPHE100electrostatic stabiliser

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PDB entries from 2024-06-12

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