Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

1NT2

CRYSTAL STRUCTURE OF FIBRILLARIN/NOP5P COMPLEX

Functional Information from GO Data
ChainGOidnamespacecontents
A0000494biological_processbox C/D sno(s)RNA 3'-end processing
A0003723molecular_functionRNA binding
A0006338biological_processchromatin remodeling
A0006364biological_processrRNA processing
A0008033biological_processtRNA processing
A0008168molecular_functionmethyltransferase activity
A0008649molecular_functionrRNA methyltransferase activity
A0016740molecular_functiontransferase activity
A0031167biological_processrRNA methylation
A0032259biological_processmethylation
A1990259molecular_functionhistone H2A Q104 methyltransferase activity
B0030515molecular_functionsnoRNA binding
B0031428cellular_componentbox C/D methylation guide snoRNP complex
B0032040cellular_componentsmall-subunit processome
Functional Information from PDB Data
site_idAC1
Number of Residues11
DetailsBINDING SITE FOR RESIDUE SAM A 301
ChainResidue
ALYS42
AILE134
AGLN136
AALA67
ATHR70
ATHR71
AGLU88
ATYR89
AASP113
AALA114
AASP133

Functional Information from PROSITE/UniProt
site_idPS00566
Number of Residues14
DetailsFIBRILLARIN Fibrillarin signature. GIIYAVEYS.AkpFE
ChainResidueDetails
AGLY82-GLU95

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsBINDING:
ChainResidueDetails
ATHR70
AGLU88
AASP113

site_idSWS_FT_FI2
Number of Residues1
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00351
ChainResidueDetails
AASP133

237423

PDB entries from 2025-06-11

PDB statisticsPDBj update infoContact PDBjnumon