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

4Z2J

Serratia marcescens Chitinase B complexed with macrolide inhibitor 31

Functional Information from GO Data
ChainGOidnamespacecontents
A0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
A0005576cellular_componentextracellular region
A0005975biological_processcarbohydrate metabolic process
A0008061molecular_functionchitin binding
A0030246molecular_functioncarbohydrate binding
Functional Information from PDB Data
site_idAC1
Number of Residues13
Detailsbinding site for residue M6G A 501
ChainResidue
ATYR10
ATRP403
AGOL503
AHOH619
AHOH690
APHE12
ATYR98
AASP142
AGLU144
AMET212
ATYR214
AASP215
ATYR292

site_idAC2
Number of Residues14
Detailsbinding site for residue M6G A 502
ChainResidue
ATRP97
AASN101
AASP102
ALEU103
AILE170
APHE190
APHE191
ATRP220
AGLU221
APHE239
AGLY480
ATYR481
AHOH602
AHOH679

site_idAC3
Number of Residues8
Detailsbinding site for residue GOL A 503
ChainResidue
APHE12
AILE13
APRO14
ATHR15
ASER50
APHE51
ATYR99
AM6G501

site_idAC4
Number of Residues3
Detailsbinding site for residue PO4 A 504
ChainResidue
AARG89
APRO178
AGLN180

site_idAC5
Number of Residues4
Detailsbinding site for residue GOL A 505
ChainResidue
AARG244
APHE259
APRO260
ASER261

Functional Information from PROSITE/UniProt
site_idPS01095
Number of Residues9
DetailsGH18_1 Glycosyl hydrolases family 18 (GH18) active site signature. FDGVDIDwE
ChainResidueDetails
APHE136-GLU144

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton donor => ECO:0000255|PROSITE-ProRule:PRU01258
ChainResidueDetails
AGLU144

site_idSWS_FT_FI2
Number of Residues5
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU01258
ChainResidueDetails
AASP68
AGLY95
ATYR145
AMET212
ATRP403

221716

PDB entries from 2024-06-26

PDB statisticsPDBj update infoContact PDBjnumon