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3BDL

Crystal structure of a truncated human Tudor-SN

Functional Information from PDB Data
site_idAC1
Number of Residues16
DetailsBINDING SITE FOR RESIDUE CIT A 2000
ChainResidue
AGLU354
AHOH2022
AHOH2027
AHOH2076
AHOH2119
AHOH2146
AHOH2174
AHOH2324
AGLY355
ATHR404
APHE510
ASER511
AARG514
AARG537
AGLY538
AARG540

site_idAC2
Number of Residues14
DetailsBINDING SITE FOR RESIDUE CIT A 2001
ChainResidue
AILE348
AARG349
AARG352
ATYR396
AARG398
ASER401
APRO402
ACYS415
AHOH2005
AHOH2028
AHOH2074
AHOH2095
AHOH2161
AHOH2451

site_idAC3
Number of Residues11
DetailsBINDING SITE FOR RESIDUE CIT A 2002
ChainResidue
AASN391
ATHR393
ATHR419
AHIS450
ALYS684
AASN688
AHOH2100
AHOH2339
AHOH2354
AHOH2409
AHOH2454

site_idAC4
Number of Residues11
DetailsBINDING SITE FOR RESIDUE CIT A 2003
ChainResidue
AARG441
AGLN442
APHE552
ASER553
AGLU554
AGLU555
AHOH2083
AHOH2112
AHOH2134
AHOH2425
AHOH2604

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569
ChainResidueDetails
ASER401

site_idSWS_FT_FI2
Number of Residues1
DetailsMOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861
ChainResidueDetails
ALYS616

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163
ChainResidueDetails
ASER620
ASER760

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569
ChainResidueDetails
ATHR754

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569
ChainResidueDetails
ASER756

site_idSWS_FT_FI6
Number of Residues2
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:28112733
ChainResidueDetails
ALYS488

226707

PDB entries from 2024-10-30

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