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4TOQ

Crystal structure of class III chitinase from pomegranate provides the insight into its metal storage capacity

Functional Information from GO Data
ChainGOidnamespacecontents
A0000272biological_processpolysaccharide catabolic process
A0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
A0004568molecular_functionchitinase activity
A0005509molecular_functioncalcium ion binding
A0005576cellular_componentextracellular region
A0005975biological_processcarbohydrate metabolic process
A0006032biological_processchitin catabolic process
A0009501cellular_componentamyloplast
A0009845biological_processseed germination
A0016787molecular_functionhydrolase activity
A0016798molecular_functionhydrolase activity, acting on glycosyl bonds
A0046872molecular_functionmetal ion binding
A0090351biological_processseedling development
B0000272biological_processpolysaccharide catabolic process
B0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
B0004568molecular_functionchitinase activity
B0005509molecular_functioncalcium ion binding
B0005576cellular_componentextracellular region
B0005975biological_processcarbohydrate metabolic process
B0006032biological_processchitin catabolic process
B0009501cellular_componentamyloplast
B0009845biological_processseed germination
B0016787molecular_functionhydrolase activity
B0016798molecular_functionhydrolase activity, acting on glycosyl bonds
B0046872molecular_functionmetal ion binding
B0090351biological_processseedling development
C0000272biological_processpolysaccharide catabolic process
C0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
C0004568molecular_functionchitinase activity
C0005509molecular_functioncalcium ion binding
C0005576cellular_componentextracellular region
C0005975biological_processcarbohydrate metabolic process
C0006032biological_processchitin catabolic process
C0009501cellular_componentamyloplast
C0009845biological_processseed germination
C0016787molecular_functionhydrolase activity
C0016798molecular_functionhydrolase activity, acting on glycosyl bonds
C0046872molecular_functionmetal ion binding
C0090351biological_processseedling development
D0000272biological_processpolysaccharide catabolic process
D0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
D0004568molecular_functionchitinase activity
D0005509molecular_functioncalcium ion binding
D0005576cellular_componentextracellular region
D0005975biological_processcarbohydrate metabolic process
D0006032biological_processchitin catabolic process
D0009501cellular_componentamyloplast
D0009845biological_processseed germination
D0016787molecular_functionhydrolase activity
D0016798molecular_functionhydrolase activity, acting on glycosyl bonds
D0046872molecular_functionmetal ion binding
D0090351biological_processseedling development
Functional Information from PDB Data
site_idAC1
Number of Residues3
Detailsbinding site for residue MG A 301
ChainResidue
ACYS50
ATHR56
CTHR56

site_idAC2
Number of Residues5
Detailsbinding site for residue MG A 302
ChainResidue
AHOH548
AHOH590
AHOH672
AHOH724
AHOH725

site_idAC3
Number of Residues4
Detailsbinding site for residue MG A 303
ChainResidue
AHOH727
AHOH728
AHOH744
AHOH625

site_idAC4
Number of Residues5
Detailsbinding site for residue MG A 304
ChainResidue
AHOH415
AHOH512
AHOH539
BHOH409
BHOH479

site_idAC5
Number of Residues3
Detailsbinding site for residue MG A 305
ChainResidue
ATHR208
ASER248
AHOH408

site_idAC6
Number of Residues2
Detailsbinding site for residue CL A 306
ChainResidue
AALA41
BALA41

site_idAC7
Number of Residues5
Detailsbinding site for residue CL A 307
ChainResidue
AASN185
APRO186
ALEU187
AALA188
AHOH436

site_idAC8
Number of Residues4
Detailsbinding site for residue MG B 301
ChainResidue
BHOH456
BHOH459
BHOH511
BHOH558

site_idAC9
Number of Residues3
Detailsbinding site for residue MG B 302
ChainResidue
BHOH596
BHOH692
BHOH696

site_idAD1
Number of Residues1
Detailsbinding site for residue CL B 303
ChainResidue
BHIS49

site_idAD2
Number of Residues4
Detailsbinding site for residue CL B 304
ChainResidue
BGLY11
BALA47
BGLY48
DGLY11

site_idAD3
Number of Residues4
Detailsbinding site for residue CL B 305
ChainResidue
BASN185
BPRO186
BLEU187
BHOH444

site_idAD4
Number of Residues5
Detailsbinding site for residue MG C 301
ChainResidue
CPRO52
CGLY55
CTHR56
CCYS57
CPRO113

site_idAD5
Number of Residues3
Detailsbinding site for residue MG C 302
ChainResidue
AHOH432
CHOH427
CHOH713

site_idAD6
Number of Residues5
Detailsbinding site for residue MG C 303
ChainResidue
CHOH513
CHOH577
CHOH578
CHOH645
CHOH662

site_idAD7
Number of Residues5
Detailsbinding site for residue MG C 304
ChainResidue
CHOH552
CHOH607
CHOH625
CHOH650
CHOH651

site_idAD8
Number of Residues4
Detailsbinding site for residue CL C 305
ChainResidue
CARG144
CHOH548
DASN102
DHOH613

site_idAD9
Number of Residues6
Detailsbinding site for residue MG D 301
ChainResidue
AARG65
CTHR146
CGLN147
CALA148
CHOH484
DSER110

site_idAE1
Number of Residues5
Detailsbinding site for residue MG D 302
ChainResidue
DHOH602
DHOH641
DHOH697
DHOH708
DHOH709

Functional Information from PROSITE/UniProt
site_idPS01095
Number of Residues9
DetailsGH18_1 Glycosyl hydrolases family 18 (GH18) active site signature. LDGIDFDiE
ChainResidueDetails
ALEU119-GLU127

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsACT_SITE: Proton donor => ECO:0000255|PROSITE-ProRule:PRU01258, ECO:0000305|PubMed:25252615
ChainResidueDetails
AGLU127
BGLU127
CGLU127
DGLU127

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PDB entries from 2024-06-12

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