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4XIK

Crystal structure of NanB sialidase from streptococcus pneumoniae in complex with DMSO

Functional Information from GO Data
ChainGOidnamespacecontents
A0004308molecular_functionexo-alpha-sialidase activity
A0005737cellular_componentcytoplasm
A0005975biological_processcarbohydrate metabolic process
A0006689biological_processganglioside catabolic process
A0009313biological_processoligosaccharide catabolic process
A0016020cellular_componentmembrane
A0016798molecular_functionhydrolase activity, acting on glycosyl bonds
A0043231cellular_componentintracellular membrane-bounded organelle
A0052794molecular_functionexo-alpha-(2->3)-sialidase activity
A0052795molecular_functionexo-alpha-(2->6)-sialidase activity
A0052796molecular_functionexo-alpha-(2->8)-sialidase activity
Functional Information from PDB Data
site_idAC1
Number of Residues7
Detailsbinding site for residue DMS A 701
ChainResidue
AARG245
AILE246
AARG264
AASP270
AILE326
AASP327
ATYR653

site_idAC2
Number of Residues4
Detailsbinding site for residue DMS A 702
ChainResidue
AGLN494
ATHR657
ATYR250
ATHR251

site_idAC3
Number of Residues5
Detailsbinding site for residue DMS A 703
ChainResidue
AGLY163
AASP217
AVAL220
AHOH1243
AHOH1250

site_idAC4
Number of Residues5
Detailsbinding site for residue DMS A 704
ChainResidue
AGLU194
AASP448
ALEU450
AHOH851
AHOH990

site_idAC5
Number of Residues4
Detailsbinding site for residue DMS A 705
ChainResidue
ASER530
AALA531
ASER532
AHOH980

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton acceptor => ECO:0000250
ChainResidueDetails
AASP270

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: ACT_SITE => ECO:0000255
ChainResidueDetails
AGLU541

site_idSWS_FT_FI3
Number of Residues1
DetailsACT_SITE: Nucleophile => ECO:0000250
ChainResidueDetails
ATYR653

site_idSWS_FT_FI4
Number of Residues3
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
AARG245
AARG557
AARG619

224572

PDB entries from 2024-09-04

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