Structure of PDB 1h0g Chain A

Receptor sequence
>1h0gA (length=496) Species: 615 (Serratia marcescens) [Search protein sequence]
TRKAVIGYYFIPTNQINNYTETDTSVVPFPVSNITPAKAKQLTHINFSFL
DINSNLECAWDPATNDAKARDVVNRLTALKAHNPSLRIMFSIGGWYYSND
LGVSHANYVNAVKTPASRTKFAQSCVRIMKDYGFDGVDIDWEYPQAAEVD
GFIAALQEIRTLLNQQTITDGRQALPYQLTIAGAGGAFFLSRYYSKLAQI
VAPLDYINLMTYDLAGPWEKVTNHQAALFGDAAGPTFYNALREANLGWSW
EELTRAFPSPFSLTVDAAVQQHLMMEGVPSAKIVMGVPFYGRAFKGVSGG
NGGQYSSHSTPGEDPYPSTDYWLVGCEECVRDKDPRIASYRQLEQMLQGN
YGYQRLWNDKTKTPYLYHAQNGLFVTYDDAESFKYKAKYIKQQQLGGVMF
WHLGQDNRNGDLLAALDRYFNAADYDDSQLDMGTGLRYTGVGPGNLPIMT
APAYVPGTTYAQGALVSYQGYVWQTKWGYITSAPGSDSAWLKVGRV
3D structure
PDB1h0g High Resolution Inhibited Complexes of a Chitinase with Natural Product Cyclopentapeptides - Peptide Mimicry of a Carbohydrate Substrate
ChainA
Resolution2.0 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D140 D142 E144 Y214
Catalytic site (residue number reindexed from 1) D138 D140 E142 Y212
Enzyme Commision number 3.2.1.14: chitinase.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 peptide A Y10 W97 E144 M212 Y214 D215 W220 Y292 R294 W403 Y8 W95 E142 M210 Y212 D213 W218 Y290 R292 W401
Gene Ontology
Molecular Function
GO:0004553 hydrolase activity, hydrolyzing O-glycosyl compounds
GO:0008061 chitin binding
GO:0030246 carbohydrate binding
Biological Process
GO:0005975 carbohydrate metabolic process
Cellular Component
GO:0005576 extracellular region

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:1h0g, PDBe:1h0g, PDBj:1h0g
PDBsum1h0g
PubMed12093900
UniProtP11797|CHIB_SERMA Chitinase B (Gene Name=chiB)

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