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3LLC

Crystal structure of Putative hydrolase (YP_002548124.1) from Agrobacterium vitis S4 at 1.80 A resolution

Functional Information from GO Data
ChainGOidnamespacecontents
A0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
A0008474molecular_functionpalmitoyl-(protein) hydrolase activity
A0016787molecular_functionhydrolase activity
A0098734biological_processmacromolecule depalmitoylation
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CL A 270
ChainResidue
ATHR52
ALYS53
AHOH319
AHOH392

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE EDO A 271
ChainResidue
AEDO272
AHOH284
ASER23
AGLN124
AVAL197
AGLY200
AMSE201

site_idAC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE EDO A 272
ChainResidue
AARG121
AGLN124
AALA194
AARG196
AEDO271
AHOH505
AHOH511

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE EDO A 273
ChainResidue
AILE123
ALEU126
AASN132
AGLN135
AVAL136
AHOH434

site_idAC5
Number of Residues3
DetailsBINDING SITE FOR RESIDUE EDO A 274
ChainResidue
AVAL28
ATHR38
APRO104

site_idAC6
Number of Residues1
DetailsBINDING SITE FOR RESIDUE EDO A 275
ChainResidue
AGLU56

site_idAC7
Number of Residues3
DetailsBINDING SITE FOR RESIDUE PEG A 276
ChainResidue
AGLU9
ATHR10
AHOH384

site_idAC8
Number of Residues5
DetailsBINDING SITE FOR RESIDUE PG4 A 277
ChainResidue
ATYR45
ASER113
AMSE114
AGLU173
AASP218

Functional Information from PROSITE/UniProt
site_idPS00136
Number of Residues11
DetailsSUBTILASE_ASP Serine proteases, subtilase family, aspartic acid active site. AGMIDTGCpv.H
ChainResidueDetails
AALA199-HIS209

221051

PDB entries from 2024-06-12

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