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4DWX

Crystal Structure of a Family GH-19 Chitinase from rye seeds

Functional Information from GO Data
ChainGOidnamespacecontents
A0000272biological_processpolysaccharide catabolic process
A0004568molecular_functionchitinase activity
A0005576cellular_componentextracellular region
A0005975biological_processcarbohydrate metabolic process
A0006032biological_processchitin catabolic process
A0008061molecular_functionchitin binding
A0016798molecular_functionhydrolase activity, acting on glycosyl bonds
A0016998biological_processcell wall macromolecule catabolic process
A0031640biological_processkilling of cells of another organism
A0050832biological_processdefense response to fungus
B0000272biological_processpolysaccharide catabolic process
B0004568molecular_functionchitinase activity
B0005576cellular_componentextracellular region
B0005975biological_processcarbohydrate metabolic process
B0006032biological_processchitin catabolic process
B0008061molecular_functionchitin binding
B0016798molecular_functionhydrolase activity, acting on glycosyl bonds
B0016998biological_processcell wall macromolecule catabolic process
B0031640biological_processkilling of cells of another organism
B0050832biological_processdefense response to fungus
Functional Information from PDB Data
site_idAC1
Number of Residues11
DetailsBINDING SITE FOR RESIDUE MES A 301
ChainResidue
AILE117
AHOH625
AHOH634
AGLN118
ALEU119
ASER120
AASN124
APHE157
AILE198
AHOH451
AHOH476

site_idAC2
Number of Residues13
DetailsBINDING SITE FOR RESIDUE SO4 A 302
ChainResidue
AHIS8
AASP12
AARG18
ATYR29
ATHR30
ATYR31
AZN304
AHOH415
AHOH423
AHOH425
AHOH589
BASP51
BHOH433

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 A 303
ChainResidue
ASER100
AGLN102
ATRP103
BSER100
BGLN102
BTRP103

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 304
ChainResidue
AHIS8
AASP12
ASO4302
BASP51

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 305
ChainResidue
AHIS17
AASP20
AHOH590
BASP232

site_idAC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN A 306
ChainResidue
AHIS121
AHOH428
AHOH479
AHOH501
BHIS206

site_idAC7
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN A 307
ChainResidue
AHIS206
AHOH532
AHOH554
AHOH618
BHIS121

site_idAC8
Number of Residues10
DetailsBINDING SITE FOR RESIDUE MES B 301
ChainResidue
BILE117
BGLN118
BLEU119
BSER120
BASN124
BILE198
BHOH440
BHOH452
BHOH490
BHOH580

site_idAC9
Number of Residues8
DetailsBINDING SITE FOR RESIDUE SO4 B 302
ChainResidue
BHIS8
BASP12
BARG18
BTHR30
BTYR31
BZN303
BHOH516
BHOH685

site_idBC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 303
ChainResidue
BHIS8
BASP12
BSO4302
BHOH467

Functional Information from PROSITE/UniProt
site_idPS00773
Number of Residues23
DetailsCHITINASE_19_1 Chitinases family 19 signature 1. Cqakg.FYTydaFVaAanaFpgFG
ChainResidueDetails
ACYS23-GLY45

site_idPS00774
Number of Residues11
DetailsCHITINASE_19_2 Chitinases family 19 signature 2. VSFkTALWFWM
ChainResidueDetails
AVAL149-MET159

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton donor => ECO:0000250|UniProtKB:P29022
ChainResidueDetails
AGLU67
BGLU67

site_idSWS_FT_FI2
Number of Residues2
DetailsSITE: May be involved in substrate-binding => ECO:0000269|Ref.5
ChainResidueDetails
ATRP72
BTRP72

site_idSWS_FT_FI3
Number of Residues2
DetailsSITE: May be involved in substrate-binding => ECO:0000269|PubMed:9532801
ChainResidueDetails
AASP95
BASP95

226707

PDB entries from 2024-10-30

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