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

5CB3

Structural Insights into the Mechanism of Escherichia coli Ymdb

Functional Information from GO Data
ChainGOidnamespacecontents
A0001883molecular_functionpurine nucleoside binding
A0008428molecular_functionribonuclease inhibitor activity
A0016787molecular_functionhydrolase activity
A0019213molecular_functiondeacetylase activity
A0019899molecular_functionenzyme binding
A0042278biological_processpurine nucleoside metabolic process
A0046677biological_processresponse to antibiotic
A0060698molecular_functionendoribonuclease inhibitor activity
A0061463molecular_functionO-acetyl-ADP-ribose deacetylase activity
A1900231biological_processregulation of single-species biofilm formation on inanimate substrate
Functional Information from PDB Data
site_idAC1
Number of Residues27
Detailsbinding site for residue APR A 401
ChainResidue
AGLY10
AVAL34
AASP35
AALA120
ASER122
ATHR123
AGLY124
AVAL125
ATYR126
ATYR159
AHOH504
AASP11
AHOH514
AHOH522
AHOH528
AHOH532
AHOH537
AHOH541
AHOH542
AHOH561
AILE12
AALA23
AASN25
AGLY30
AGLY31
AGLY32
AGLY33

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton acceptor => ECO:0000255|HAMAP-Rule:MF_01205, ECO:0000305|PubMed:26481419
ChainResidueDetails
AASP35

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01205, ECO:0000269|PubMed:26481419
ChainResidueDetails
AASP11
AASN25
AGLY33
ASER122

227111

PDB entries from 2024-11-06

PDB statisticsPDBj update infoContact PDBjnumon