BioLiP

Structure of PDB 1gor Chain A

Receptor sequence

>1gorA (length=302) Species: 5087 (Thermoascus aurantiacus) [Search protein sequence]

EAAQSVDQLIKARGKVYFGVATDQNRLTTGKNAAIIQADFGQVTPENSMK
WDATEPSQGNFNFAGADYLVNWAQQNGKLIRGHTLVWHSQLPSWVSSITD
KNTLTNVMKNHITTLMTRYKGKIRAWDVVNEAFNEDGSLRQTVFLNVIGE
DYIPIAFQTARAADPNAKLYINDYNLDSASYPKTQAIVNRVKQWRAAGVP
IDGIGSQTHLSAGQGAGVLQALPLLASAGTPEVAITELDVAGASPTDYVN
VVNACLNVQSCVGITVWGVADPDSWRASTTPLLFDGNFNPKPAYNAIVQD
LQ

3D structure

PDB

1gor Substrate Specificity and Subsite Mobility in T. Aurantiacus Xylanase 10A

Chain

Resolution

1.7 Å

3D
structure

Catalytic site residues are labeled in the structure
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Enzymatic activity

Catalytic site (original residue number in PDB)	E131 N172 H209 E237 D239
Catalytic site (residue number reindexed from 1)	E131 N172 H209 E237 D239
Enzyme Commision number	3.2.1.8: endo-1,4-beta-xylanase.

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	XYS	A	K50 H83 W87 N130 Q207 H209 E237 W267 W275 Q302	K50 H83 W87 N130 Q207 H209 E237 W267 W275 Q302
BS02	XYP	A	E46 N47 K50 Q90 W267	E46 N47 K50 Q90 W267

Gene Ontology

	Molecular Function
GO:0004553	hydrolase activity, hydrolyzing O-glycosyl compounds
GO:0016798	hydrolase activity, acting on glycosyl bonds
GO:0031176	endo-1,4-beta-xylanase activity

	Biological Process
GO:0005975	carbohydrate metabolic process
GO:0045493	xylan catabolic process

View graph for
Molecular Function

View graph for
Biological Process

PDB	RCSB:1gor, PDBe:1gor, PDBj:1gor
PDBsum	1gor
PubMed	11741607
UniProt	P23360\|XYNA_THEAU Endo-1,4-beta-xylanase (Gene Name=XYNA)