4KC7

Crystal Structure of Endo-1,5-alpha-L-arabinanase from Thermotoga petrophila RKU-1

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	0031222	biological_process	arabinan catabolic process
A	0046558	molecular_function	arabinan endo-1,5-alpha-L-arabinosidase activity
A	0046872	molecular_function	metal ion binding
B	0004553	molecular_function	hydrolase activity, hydrolyzing O-glycosyl compounds
B	0005576	cellular_component	extracellular region
B	0005975	biological_process	carbohydrate metabolic process
B	0016798	molecular_function	hydrolase activity, acting on glycosyl bonds
B	0031222	biological_process	arabinan catabolic process
B	0046558	molecular_function	arabinan endo-1,5-alpha-L-arabinosidase activity
B	0046872	molecular_function	metal ion binding
C	0004553	molecular_function	hydrolase activity, hydrolyzing O-glycosyl compounds
C	0005576	cellular_component	extracellular region
C	0005975	biological_process	carbohydrate metabolic process
C	0016798	molecular_function	hydrolase activity, acting on glycosyl bonds
C	0031222	biological_process	arabinan catabolic process
C	0046558	molecular_function	arabinan endo-1,5-alpha-L-arabinosidase activity
C	0046872	molecular_function	metal ion binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE PEG A 501

Chain	Residue
A	HIS31
A	HIS48
A	PHE116
A	TYR341

---

site_id	AC2
Number of Residues	7
Details	BINDING SITE FOR RESIDUE CA A 502

Chain	Residue
A	HOH940
A	HOH942
A	HIS314
A	HOH929
A	HOH930
A	HOH931
A	HOH932

---

site_id	AC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE PEG B 501

Chain	Residue
B	HIS31
B	HIS48
B	TRP95
B	PHE116
B	TYR341

---

site_id	AC4
Number of Residues	7
Details	BINDING SITE FOR RESIDUE PEG B 502

Chain	Residue
B	ASN384
B	GLU428
B	VAL433
B	TYR435
B	SER458
B	GLN460
B	VAL462

---

site_id	AC5
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CA B 503

Chain	Residue
B	HIS314
B	HOH758
B	HOH772
B	HOH773
B	HOH774

---

site_id	AC6
Number of Residues	3
Details	BINDING SITE FOR RESIDUE PEG C 501

Chain	Residue
C	TYR148
C	SER149
C	GLY152

---

site_id	AC7
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CA C 502

Chain	Residue
C	HIS314
C	HOH774
C	HOH776
C	HOH796

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	3
Details	ACT_SITE: Proton acceptor => ECO:0000305|PubMed:24469445

Chain	Residue	Details
A	ASP32
B	ASP32
C	ASP32

---

site_id	SWS_FT_FI2
Number of Residues	3
Details	ACT_SITE: Proton donor => ECO:0000305|PubMed:24469445

Chain	Residue	Details
A	GLU223
B	GLU223
C	GLU223

---

site_id	SWS_FT_FI3
Number of Residues	15
Details	BINDING: BINDING => ECO:0000250

Chain	Residue	Details
A	ASP32
B	HIS314
C	ASP32
C	ASN167
C	SER187
C	HIS219
C	HIS314
A	ASN167
A	SER187
A	HIS219
A	HIS314
B	ASP32
B	ASN167
B	SER187
B	HIS219

---

site_id	SWS_FT_FI4
Number of Residues	3
Details	BINDING: BINDING => ECO:0000305|PubMed:24469445

Chain	Residue	Details
A	GLY117
B	GLY117
C	GLY117

---

site_id	SWS_FT_FI5
Number of Residues	3
Details	SITE: Important for catalytic activity => ECO:0000250

Chain	Residue	Details
A	ASP170
B	ASP170
C	ASP170

---

site_id	SWS_FT_FI6
Number of Residues	3
Details	SITE: Important for substrate recognition => ECO:0000250

Chain	Residue	Details
A	HIS314
B	HIS314
C	HIS314

---