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7SE7

Crystal structure of human Fibrillarin in complex with S-adenosyl-L-methionine

Functional Information from GO Data
ChainGOidnamespacecontents
A0003723molecular_functionRNA binding
A0006364biological_processrRNA processing
A0008168molecular_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 Residues1
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:Q9Y9U3
ChainResidueDetails
ATHR172

site_idSWS_FT_FI2
Number of Residues3
DetailsBINDING: BINDING => ECO:0000269|Ref.31
ChainResidueDetails
AASP236
AGLU191
AASP216

site_idSWS_FT_FI3
Number of Residues4
DetailsMOD_RES: N6-acetyllysine => ECO:0000269|PubMed:30540930
ChainResidueDetails
ALYS121
ALYS205
ALYS206
ALYS102

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163
ChainResidueDetails
ASER126
ASER116

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569
ChainResidueDetails
ASER124

site_idSWS_FT_FI6
Number of Residues7
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:28112733
ChainResidueDetails
ALYS84
ALYS102
ALYS109
ALYS131
ALYS143
ALYS158

221051

PDB entries from 2024-06-12

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