3LGR

Xylanase II from Trichoderma reesei cocrystallized with tris-dipicolinate europium

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004553	molecular_function	hydrolase activity, hydrolyzing O-glycosyl compounds
A	0005576	cellular_component	extracellular region
A	0005975	biological_process	carbohydrate metabolic process
A	0016798	molecular_function	hydrolase activity, acting on glycosyl bonds
A	0031176	molecular_function	endo-1,4-beta-xylanase activity
A	0045493	biological_process	xylan catabolic process

Functional Information from PDB Data

site_id	AC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE EU A 201

Chain	Residue
A	PDC302
A	PDC302
A	PDC303
A	PDC303
A	PDC304
A	PDC304

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site_id	AC2
Number of Residues	1
Details	BINDING SITE FOR RESIDUE EU A 202

Chain	Residue
A	HOH229

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site_id	AC3
Number of Residues	2
Details	BINDING SITE FOR RESIDUE EU A 203

Chain	Residue
A	HOH331
A	HOH544

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site_id	AC4
Number of Residues	16
Details	BINDING SITE FOR RESIDUE PDC A 302

Chain	Residue
A	GLN4
A	PRO5
A	ASN19
A	GLY21
A	HIS22
A	GLY23
A	GLY23
A	GLY24
A	EU201
A	EU201
A	PDC303
A	PDC303
A	PDC304
A	PDC304
A	HOH383
A	HOH514

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site_id	AC5
Number of Residues	15
Details	BINDING SITE FOR RESIDUE PDC A 303

Chain	Residue
A	GLN4
A	PRO5
A	ASN19
A	GLY21
A	HIS22
A	GLY23
A	GLY24
A	EU201
A	EU201
A	PDC302
A	PDC302
A	PDC304
A	PDC304
A	HOH383
A	HOH514

---

site_id	AC6
Number of Residues	18
Details	BINDING SITE FOR RESIDUE PDC A 304

Chain	Residue
A	ILE3
A	ILE3
A	GLN4
A	GLN4
A	TYR17
A	TYR17
A	VAL25
A	VAL25
A	EU201
A	EU201
A	PDC302
A	PDC302
A	PDC303
A	PDC303
A	HOH351
A	HOH351
A	HOH395
A	HOH395

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Functional Information from PROSITE/UniProt

site_id	PS00776
Number of Residues	11
Details	GH11_1 Glycosyl hydrolases family 11 (GH11) active site signature 1. PLiEYYIVEnF

Chain	Residue	Details
A	PRO83-PHE93

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site_id	PS00777
Number of Residues	12
Details	GH11_2 Glycosyl hydrolases family 11 (GH11) active site signature 2. VavEGYFSSGsA

Chain	Residue	Details
A	VAL174-ALA185

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	ACT_SITE: Nucleophile => ECO:0000269|PubMed:26392527, ECO:0000305|PubMed:24419374

Chain	Residue	Details
A	TYR87

---

site_id	SWS_FT_FI2
Number of Residues	1
Details	ACT_SITE: Proton donor => ECO:0000269|PubMed:26392527, ECO:0000305|PubMed:24419374

Chain	Residue	Details
A	GLY178

---

site_id	SWS_FT_FI3
Number of Residues	7
Details	BINDING: BINDING => ECO:0000269|PubMed:24419374

Chain	Residue	Details
A	LEU74
A	GLY78
A	ILE89
A	VAL123
A	SER127
A	TYR137
A	GLN172

---

site_id	SWS_FT_FI4
Number of Residues	1
Details	MOD_RES: Pyrrolidone carboxylic acid => ECO:0000269|PubMed:1369024, ECO:0000269|PubMed:16790934

Chain	Residue	Details
A	THR2

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site_id	SWS_FT_FI5
Number of Residues	2
Details	CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255

Chain	Residue	Details
A	TRP39
A	PHE62

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