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

5NPE

Crystal Structure of cjAgd31B (alpha-transglucosylase from Glycoside Hydrolase Family 31) in complex with beta Cyclophellitol Aziridine probe KY358

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
A0005975biological_processcarbohydrate metabolic process
A0016757molecular_functionglycosyltransferase activity
A0030246molecular_functioncarbohydrate binding
A0033825molecular_functionoligosaccharide 4-alpha-D-glucosyltransferase activity
Functional Information from PDB Data
site_idAC1
Number of Residues6
Detailsbinding site for residue SO4 A 901
ChainResidue
ATHR323
APRO324
ALEU325
AASP326
AHOH1183
AHOH1298

site_idAC2
Number of Residues3
Detailsbinding site for residue SO4 A 902
ChainResidue
AARG58
AARG231
AHOH1312

site_idAC3
Number of Residues5
Detailsbinding site for residue SO4 A 903
ChainResidue
ATHR732
AASP733
AASN734
AGLN735
AHOH1011

site_idAC4
Number of Residues4
Detailsbinding site for residue SO4 A 904
ChainResidue
AASP553
AGLU554
AARG797
AHOH1357

site_idAC5
Number of Residues5
Detailsbinding site for residue SO4 A 905
ChainResidue
AGLY239
AASN240
ASER244
AASN248
AHOH1316

site_idAC6
Number of Residues5
Detailsbinding site for residue SO4 A 906
ChainResidue
ATHR97
AGLU98
AASN99
AHIS100
AGLN703

site_idAC7
Number of Residues5
Detailsbinding site for residue PG4 A 907
ChainResidue
AARG569
ATYR674
AGLU690
AHOH1003
AHOH1455

site_idAC8
Number of Residues4
Detailsbinding site for residue EDO A 908
ChainResidue
ALYS360
AGLU809
AALA810
AHOH1237

site_idAC9
Number of Residues6
Detailsbinding site for residue EDO A 909
ChainResidue
AARG270
AGLU278
ATHR787
APRO788
AHOH1126
AHOH1185

site_idAD1
Number of Residues14
Detailsbinding site for residue 948 A 910
ChainResidue
APHE271
AASP299
AILE341
ATRP410
AASP412
ALEU413
AARG463
ATRP477
AASP480
APHE513
AHIS540
AHOH1038
AHOH1069
AHOH1244

site_idAD2
Number of Residues5
Detailsbinding site for residue OXL A 911
ChainResidue
ASER764
AGLN766
ALYS817
AHOH1147
AHOH1252

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Nucleophile => ECO:0000269|PubMed:23132856
ChainResidueDetails
AASP412

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: ACT_SITE => ECO:0000250|UniProtKB:P31434
ChainResidueDetails
AGLU415

site_idSWS_FT_FI3
Number of Residues1
DetailsACT_SITE: Proton donor => ECO:0000250|UniProtKB:P31434
ChainResidueDetails
AASP480

site_idSWS_FT_FI4
Number of Residues5
DetailsBINDING: BINDING => ECO:0000269|PubMed:23132856
ChainResidueDetails
AASP299
AGLU417
AARG463
AASP480
AHIS540

226707

PDB entries from 2024-10-30

PDB statisticsPDBj update infoContact PDBjnumon