Structure of PDB 5gy0 Chain A

Receptor sequence

>5gy0A (length=599) Species: 1515 (Acetivibrio thermocellus)

SYNYAEALQKAIYFYECQQAGPLPEWNRVEWRGDATMNDEVLGGWYDAGD
HVKFNLPMAYSAAMLGWALYEYGDDIEASGQRLHLERNLAFALDYLVACD
RGDSVVYQIGDGAADHKWWGSAEVIEKEMTRPYFVGKGSAVVGQMAAALA
VGSIVLKNDTYLRYAKKYFELADATRSDSTYTAANGFYSSHSGFWDELLW
ASTWLYLATGDRNYLDKAESYTPKLNRQNQTTDIEYQWAHCWDDCHYGAM
ILLARATGKEEYHKFAQMHLDWWTPQGYNGKRVAYTPGGLAHLDTWGPLR
YATTEAFLAFVYADSINDPALKQKYYNFAKSQIDYALGSNPDNRSYVVGF
GNNPPQRPHHRTAHGTWLDKRDIPEKHRHVLYGALVGGPGRDDSYEDNIE
DYVKNAVACDYNAGFVGALCRLTAEYGGTPLANFPPPEQRDDEFFVEAAI
NQASDHFTEIKALLNNRSSWPARLIKDLSYNYYMDLTEVFEAGYSVDDIK
VTIGYCESGMDVEISPITHLYDNIYYIKISYIDGTNICPIGQEQYAAELQ
FRIAAPQGTKFWDPTNDFSYQGLTRELAKTKYMPVFDGATKIFGEVPGG

3D structure

• PDB: 5gy0 Crystal Structures of the C-Terminally Truncated Endoglucanase Cel9Q from Clostridium thermocellum Complexed with Cellodextrins and Tris.
• Chain: A
• Resolution: 1.74 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): D76 D79 Y217 A435
• Catalytic site (residue number reindexed from 1): D47 D50 Y188 A406
• Enzyme Commision number: 3.2.1.-

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	BGC	A	H145 F216 Y217 W325 Y440	H116 F187 Y188 W296 Y411
BS02	BGC	A	F216 R329	F187 R300
BS03	BGC	A	H220 W267 C270 W271 Y330	H191 W238 C241 W242 Y301
BS04	BGC	A	E264 W267 D272	E235 W238 D243
BS05	CA	A	S221 G222 D225 E226 D272	S192 G193 D196 E197 D243
BS06	CA	A	D514 E517 D592 N595 D596	D485 E488 D563 N566 D567

Gene Ontology

Molecular Function

• GO:0004553 hydrolase activity, hydrolyzing O-glycosyl compounds
• GO:0030246 carbohydrate binding
• GO:0030248 cellulose binding

Biological Process

• GO:0005975 carbohydrate metabolic process

External links

• PDB: RCSB:5gy0, PDBe:5gy0, PDBj:5gy0
• PDBsum: 5gy0
• PubMed: 30609216
• UniProt: Q9AJF8