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5NPC

Crystal Structure of D412N nucleophile mutant cjAgd31B (alpha-transglucosylase from Glycoside Hydrolase Family 31) in complex with unreacted alpha Cyclophellitol Cyclosulfate probe ME647

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
A0005975biological_processcarbohydrate metabolic process
A0006491biological_processN-glycan processing
A0016757molecular_functionglycosyltransferase activity
A0030246molecular_functioncarbohydrate binding
A0033825molecular_functionoligosaccharide 4-alpha-D-glucosyltransferase activity
A0090599molecular_functionalpha-glucosidase activity
Functional Information from PDB Data
site_idAC1
Number of Residues4
Detailsbinding site for residue SO4 A 901
ChainResidue
ATHR323
APRO324
ALEU325
AASP326

site_idAC2
Number of Residues3
Detailsbinding site for residue SO4 A 902
ChainResidue
AARG58
APRO79
AARG231

site_idAC3
Number of Residues4
Detailsbinding site for residue SO4 A 903
ChainResidue
AARG797
AHOH1193
AASP553
AGLU554

site_idAC4
Number of Residues4
Detailsbinding site for residue SO4 A 904
ChainResidue
ATHR732
AASP733
AASN734
AGLN735

site_idAC5
Number of Residues4
Detailsbinding site for residue SO4 A 905
ChainResidue
ATHR97
AGLU98
AASN99
AHIS100

site_idAC6
Number of Residues5
Detailsbinding site for residue SO4 A 906
ChainResidue
ALYS358
AARG753
AGLY807
AARG808
AGLU809

site_idAC7
Number of Residues6
Detailsbinding site for residue SO4 A 907
ChainResidue
ATHR107
AASP124
AGLY239
AASN240
ASER244
AASN248

site_idAC8
Number of Residues2
Detailsbinding site for residue SO4 A 908
ChainResidue
AARG274
AHOH1165

site_idAC9
Number of Residues5
Detailsbinding site for residue EDO A 909
ChainResidue
AGLU276
AARG280
ATHR805
AHOH1012
AHOH1208

site_idAD1
Number of Residues2
Detailsbinding site for residue EDO A 910
ChainResidue
AASP683
AARG685

site_idAD2
Number of Residues1
Detailsbinding site for residue EDO A 911
ChainResidue
AARG590

site_idAD3
Number of Residues3
Detailsbinding site for residue EDO A 912
ChainResidue
AGLU278
ATHR787
APRO788

site_idAD4
Number of Residues2
Detailsbinding site for residue EDO A 913
ChainResidue
APHE373
AGLU374

site_idAD5
Number of Residues3
Detailsbinding site for residue EDO A 914
ChainResidue
AGLN77
ALEU78
AGLY230

site_idAD6
Number of Residues4
Detailsbinding site for residue EDO A 915
ChainResidue
AARG176
AALA177
AHIS178
AGLN187

site_idAD7
Number of Residues6
Detailsbinding site for residue EDO A 916
ChainResidue
ATRP316
ALYS318
ALYS351
ALYS351
AHOH1138
AHOH1255

site_idAD8
Number of Residues5
Detailsbinding site for residue EDO A 917
ChainResidue
ALYS305
ALYS305
AHIS310
AGLU319
AHOH1085

site_idAD9
Number of Residues1
Detailsbinding site for residue EDO A 918
ChainResidue
APHE386

site_idAE1
Number of Residues2
Detailsbinding site for residue EDO A 919
ChainResidue
AGLU64
AGLN251

site_idAE2
Number of Residues2
Detailsbinding site for residue PG4 A 921
ChainResidue
AARG569
ATYR674

site_idAE3
Number of Residues12
Detailsbinding site for residue 94E A 922
ChainResidue
APHE271
AASP299
AILE341
ATRP410
AASN412
AARG463
AASP480
APHE513
AHIS540
AGLN542
AHOH1055
AHOH1109

site_idAE4
Number of Residues5
Detailsbinding site for residue OXL A 923
ChainResidue
ASER764
AARG798
ALYS817
AHOH1125
AHOH1135

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Nucleophile => ECO:0000269|PubMed:23132856
ChainResidueDetails
AASN412

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

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PDB entries from 2024-06-12

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