Structure of PDB 1ffq Chain A

Receptor sequence
>1ffqA (length=540) Species: 615 (Serratia marcescens) [Search protein sequence]
AAPGKPTIAWGNTKFAIVEVDQAATAYNNLVKVKNAADVSVSWNLWNGDT
GTTAKVLLNGKEAWSGPSTGSSGTANFKVNKGGRYQMQVALCNADGCTAS
DATEIVVADTDGSHLAPLKEPLLEKNKPYKQNSGKVVGSYFVEWGVYGRN
FTVDKIPAQNLTHLLYGFIPICGGNGINDSLKEIEGSFQALQRSCQGRED
FKVSIHDPFAALQKAQKGVTAWDDPYKGNFGQLMALKQAHPDLKILPSIG
GWTLSDPFFFMGDKVKRDRFVGSVKEFLQTWKFFDGVDIDWEFPGGKGAN
PNLGSPQDGETYVLLMKELRAMLDQLSVETGRKYELTSAISAGKDKIDKV
AYNVAQNSMDHIFLMSYDFYGAFDLKNLGHQTALNAPAWKPDTAYTTVNG
VNALLAQGVKPGKIVVGTAMYGRGWTGVNGYQNNIPFTGTATGPVKGTWE
NGIVDYRQIAGQFMSGEWQYTYDATAEAPYVFKPSTGDLITFDDARSVQA
KGKYVLDKQLGGLFSWEIDADNGDILNSMNASLGNSAGVQ
3D structure
PDB1ffq De novo purification scheme and crystallization conditions yield high-resolution structures of chitinase A and its complex with the inhibitor allosamidin.
ChainA
Resolution1.9 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D311 D313 E315 Y390
Catalytic site (residue number reindexed from 1) D288 D290 E292 Y367
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 AMI A Y163 F191 W275 D313 E315 M388 D391 Y444 W539 Y140 F168 W252 D290 E292 M365 D368 Y421 W516
Gene Ontology
Molecular Function
GO:0004553 hydrolase activity, hydrolyzing O-glycosyl compounds
GO:0004568 chitinase activity
GO:0008061 chitin binding
GO:0016798 hydrolase activity, acting on glycosyl bonds
Biological Process
GO:0000272 polysaccharide catabolic process
GO:0005975 carbohydrate metabolic process
GO:0006032 chitin catabolic process

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Molecular Function
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Biological Process
External links
PDB RCSB:1ffq, PDBe:1ffq, PDBj:1ffq
PDBsum1ffq
PubMed12554965
UniProtP07254|CHIA_SERMA Chitinase A (Gene Name=chiA)

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