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

7SEC

Crystal structure of human Fibrillarin in complex with compound 1a

Functional Information from GO Data
ChainGOidnamespacecontents
A0003723molecular_functionRNA binding
A0006364biological_processrRNA processing
A0008168molecular_functionmethyltransferase activity
B0003723molecular_functionRNA binding
B0006364biological_processrRNA processing
B0008168molecular_functionmethyltransferase activity
Functional Information from PROSITE/UniProt
site_idPS00566
Number of Residues15
DetailsFIBRILLARIN Fibrillarin signature. GLVYAVEFShRsgRD
ChainResidueDetails
AGLY185-ASP199

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:Q9Y9U3
ChainResidueDetails
ATHR172
BTHR172

site_idSWS_FT_FI2
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|Ref.31
ChainResidueDetails
BASP216
BASP236
AGLU191
AASP216
AASP236
BGLU191

site_idSWS_FT_FI3
Number of Residues8
DetailsMOD_RES: N6-acetyllysine => ECO:0000269|PubMed:30540930
ChainResidueDetails
ALYS205
ALYS206
BLYS102
BLYS121
BLYS205
BLYS206
ALYS102
ALYS121

site_idSWS_FT_FI4
Number of Residues4
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163
ChainResidueDetails
ASER126
ASER116
BSER116
BSER126

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569
ChainResidueDetails
ASER124
BSER124

site_idSWS_FT_FI6
Number of Residues14
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:28112733
ChainResidueDetails
ALYS84
ALYS102
ALYS109
ALYS131
ALYS143
ALYS158
BLYS84
BLYS102
BLYS109
BLYS131
BLYS143
BLYS158

221051

PDB entries from 2024-06-12

PDB statisticsPDBj update infoContact PDBjnumon