Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

3SYU

Re-refined coordinates for pdb entry 1det - ribonuclease T1 carboxymethylated at GLU 58 in complex 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
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE NA A 106
ChainResidue
AGLY30
AHIS92
AALA95
AHOH206
AHOH236
AHOH992

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE NA A 107
ChainResidue
AHOH256
AHOH268
ATHR32
ATYR45
AHOH220

site_idAC3
Number of Residues13
DetailsBINDING SITE FOR RESIDUE 2GP A 105
ChainResidue
ATYR42
AASN43
AASN44
ATYR45
AGLU46
ACGA58
AASN98
AASN98
APHE100
AHOH231
AHOH258
AHOH260
AHOH267

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
ACGA58

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
AHIS40proton shuttle (general acid/base)
ACGA58proton shuttle (general acid/base)
AARG77electrostatic stabiliser
AHIS92proton shuttle (general acid/base)
APHE100electrostatic stabiliser

218853

PDB entries from 2024-04-24

PDB statisticsPDBj update infoContact PDBjnumon