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

5VLQ

Structure of the TTLL3 Glycylase

Functional Information from GO Data
ChainGOidnamespacecontents
A0036211biological_processprotein modification process
B0036211biological_processprotein modification process
Functional Information from PDB Data
site_idAC1
Number of Residues4
Detailsbinding site for residue ANP A 601
ChainResidue
AGLN372
ALYS373
AILE375
AGLN520

site_idAC2
Number of Residues3
Detailsbinding site for residue SO4 A 602
ChainResidue
AARG389
APRO525
ATHR526

site_idAC3
Number of Residues6
Detailsbinding site for residue ANP B 601
ChainResidue
BTYR374
BILE375
BMET509
BGLN520
BGLN372
BLYS373

site_idAC4
Number of Residues4
Detailsbinding site for residue SO4 B 602
ChainResidue
BARG389
BARG411
BPRO525
BTHR526

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues16
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:A4Q9E8
ChainResidueDetails
BGLN520
BASN522
ASER432
AASP507
AGLN520
AASN522
BLYS334
BARG340
BLYS385
BCYS429
BSER432
BASP507
ALYS334
AARG340
ALYS385
ACYS429

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:28576883, ECO:0007744|PDB:5VLQ
ChainResidueDetails
AGLN372
BGLN372

site_idSWS_FT_FI3
Number of Residues2
DetailsSITE: Essential for specifying initiation versus elongation step of the polyglycylase activity => ECO:0000250|UniProtKB:A4Q9E8
ChainResidueDetails
AARG340
BARG340

221051

PDB entries from 2024-06-12

PDB statisticsPDBj update infoContact PDBjnumon