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3HOH

RIBONUCLEASE T1 (THR93GLN MUTANT) COMPLEXED WITH 2'GMP

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
B0001411cellular_componenthyphal tip
B0003723molecular_functionRNA binding
B0004518molecular_functionnuclease activity
B0004519molecular_functionendonuclease activity
B0004540molecular_functionRNA nuclease activity
B0008150biological_processbiological_process
B0016787molecular_functionhydrolase activity
B0016829molecular_functionlyase activity
B0030428cellular_componentcell septum
B0046589molecular_functionribonuclease T1 activity
C0001411cellular_componenthyphal tip
C0003723molecular_functionRNA binding
C0004518molecular_functionnuclease activity
C0004519molecular_functionendonuclease activity
C0004540molecular_functionRNA nuclease activity
C0008150biological_processbiological_process
C0016787molecular_functionhydrolase activity
C0016829molecular_functionlyase activity
C0030428cellular_componentcell septum
C0046589molecular_functionribonuclease T1 activity
D0001411cellular_componenthyphal tip
D0003723molecular_functionRNA binding
D0004518molecular_functionnuclease activity
D0004519molecular_functionendonuclease activity
D0004540molecular_functionRNA nuclease activity
D0008150biological_processbiological_process
D0016787molecular_functionhydrolase activity
D0016829molecular_functionlyase activity
D0030428cellular_componentcell septum
D0046589molecular_functionribonuclease T1 activity
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA C 105
ChainResidue
CGLY47
CASP49
CHOH379
DTYR45
DHOH351
DHOH434

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA D 106
ChainResidue
CTYR45
CHOH406
CHOH420
CHOH487
DGLY47
DASP49

site_idAC3
Number of Residues14
DetailsBINDING SITE FOR RESIDUE 2GP A 107
ChainResidue
AASN36
ATYR38
AHIS40
ALYS41
ATYR42
AASN43
AASN44
ATYR45
AGLU46
AGLU58
AASN98
APHE100
AHOH331
AHOH369

site_idAC4
Number of Residues14
DetailsBINDING SITE FOR RESIDUE 2GP B 108
ChainResidue
BTYR38
BHIS40
BLYS41
BTYR42
BASN43
BASN44
BTYR45
BGLU46
BGLU58
BARG77
BHIS92
BASN98
BPHE100
BHOH402

site_idAC5
Number of Residues14
DetailsBINDING SITE FOR RESIDUE 2GP C 109
ChainResidue
ASER53
CHIS40
CLYS41
CTYR42
CASN43
CASN44
CTYR45
CGLU46
CASN99
CPHE100
CHOH314
CHOH335
CHOH523
CHOH525

site_idAC6
Number of Residues23
DetailsBINDING SITE FOR RESIDUE 2GP C 110
ChainResidue
AASN81
AGLU82
AASN83
CASN36
CTYR38
CHIS40
CGLU58
CSER72
CPRO73
CGLY74
CARG77
CHIS92
CASN98
CPHE100
CHOH314
CHOH335
CHOH384
CHOH401
CHOH444
CHOH465
ASER53
ASER54
APRO55

site_idAC7
Number of Residues13
DetailsBINDING SITE FOR RESIDUE 2GP D 111
ChainResidue
DTYR38
DHIS40
DLYS41
DTYR42
DASN43
DASN44
DTYR45
DGLU46
DGLU58
DASN98
DPHE100
DHOH395
DHOH528

site_idBI1
Number of Residues5
DetailsBINDING SITE.
ChainResidue
ATYR42
AASN43
AASN44
ATYR45
AGLU46

site_idBI2
Number of Residues5
DetailsBINDING SITE.
ChainResidue
BTYR42
BASN43
BASN44
BTYR45
BGLU46

site_idBI3
Number of Residues5
DetailsBINDING SITE.
ChainResidue
CTYR42
CASN43
CASN44
CTYR45
CGLU46

site_idBI4
Number of Residues5
DetailsBINDING SITE.
ChainResidue
DTYR42
DASN43
DASN44
DTYR45
DGLU46

site_idCA1
Number of Residues1
DetailsSITE.
ChainResidue
CASP49

site_idCA2
Number of Residues1
DetailsSITE.
ChainResidue
DASP49

site_idCT1
Number of Residues5
DetailsACTIVE SITE.
ChainResidue
ATYR38
AHIS40
AGLU58
AARG77
AHIS92

site_idCT2
Number of Residues5
DetailsACTIVE SITE.
ChainResidue
BHIS92
BTYR38
BHIS40
BGLU58
BARG77

site_idCT3
Number of Residues5
DetailsACTIVE SITE.
ChainResidue
CTYR38
CHIS40
CGLU58
CARG77
CHIS92

site_idCT4
Number of Residues5
DetailsACTIVE SITE.
ChainResidue
DTYR38
DHIS40
DGLU58
DARG77
DHIS92

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsACT_SITE: ACT_SITE => ECO:0000269|PubMed:2844811
ChainResidueDetails
AHIS40
BHIS40
CHIS40
DHIS40

site_idSWS_FT_FI2
Number of Residues4
DetailsACT_SITE: Proton acceptor => ECO:0000269|PubMed:2844811
ChainResidueDetails
AGLU58
BGLU58
CGLU58
DGLU58

site_idSWS_FT_FI3
Number of Residues4
DetailsACT_SITE: Proton donor
ChainResidueDetails
AHIS92
BHIS92
CHIS92
DHIS92

Catalytic Information from CSA
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
BTYR38electrostatic stabiliser
BHIS40proton shuttle (general acid/base)
BGLU58proton shuttle (general acid/base)
BARG77electrostatic stabiliser
BHIS92proton shuttle (general acid/base)
BPHE100electrostatic stabiliser

site_idMCSA3
Number of Residues6
DetailsM-CSA 414
ChainResidueDetails
CTYR38electrostatic stabiliser
CHIS40proton shuttle (general acid/base)
CGLU58proton shuttle (general acid/base)
CARG77electrostatic stabiliser
CHIS92proton shuttle (general acid/base)
CPHE100electrostatic stabiliser

site_idMCSA4
Number of Residues6
DetailsM-CSA 414
ChainResidueDetails
DTYR38electrostatic stabiliser
DHIS40proton shuttle (general acid/base)
DGLU58proton shuttle (general acid/base)
DARG77electrostatic stabiliser
DHIS92proton shuttle (general acid/base)
DPHE100electrostatic stabiliser

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PDB entries from 2024-04-24

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