6KW9

Crystal Structure Analysis of Endo-beta-1,4-xylanase II Complexed with Xylotriose

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000272	biological_process	polysaccharide catabolic process
A	0004553	molecular_function	hydrolase activity, hydrolyzing O-glycosyl compounds
A	0005576	cellular_component	extracellular region
A	0005975	biological_process	carbohydrate metabolic process
A	0016787	molecular_function	hydrolase activity
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	8
Details	binding site for residue GOL A 201

Chain	Residue
A	ASN61
A	SER63
A	ASN82
A	PRO83
A	THR188
A	VAL189
A	SER190
A	HOH302

---

site_id	AC2
Number of Residues	6
Details	binding site for residue GOL A 202

Chain	Residue
A	GLY24
A	VAL25
A	LYS56
A	HOH420
A	HOH459
A	GLY23

---

site_id	AC3
Number of Residues	1
Details	binding site for residue IOD A 203

Chain	Residue
A	GLY112

---

site_id	AC4
Number of Residues	2
Details	binding site for residue IOD A 204

Chain	Residue
A	VAL114
A	ARG142

---

site_id	AC5
Number of Residues	2
Details	binding site for residue IOD A 205

Chain	Residue
A	VAL123
A	GLN125

---

site_id	AC6
Number of Residues	3
Details	binding site for residue IOD A 206

Chain	Residue
A	THR28
A	GLN34
A	SER36

---

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

---

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

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	Active site: {"description":"Nucleophile","evidences":[{"source":"PubMed","id":"26392527","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"24419374","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	1
Details	Active site: {"description":"Proton donor","evidences":[{"source":"PubMed","id":"26392527","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"24419374","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	7
Details	Binding site: {"evidences":[{"source":"PubMed","id":"24419374","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	2
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---