3CBH

THREE-DIMENSIONAL STRUCTURE OF CELLOBIOHYDROLASE FROM TRICHODERMA REESEI

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004553	molecular_function	hydrolase activity, hydrolyzing O-glycosyl compounds
A	0005975	biological_process	carbohydrate metabolic process
A	0030245	biological_process	cellulose catabolic process

Functional Information from PROSITE/UniProt

site_id	PS00655
Number of Residues	17
Details	GLYCOSYL_HYDROL_F6_1 Glycosyl hydrolases family 6 signature 1. VvYdlPdRDCAalASnG

Chain	Residue	Details
A	VAL167-GLY183

---

site_id	PS00656
Number of Residues	10
Details	GLYCOSYL_HYDROL_F6_2 Glycosyl hydrolases family 6 signature 2. LLVIEPDSLA

Chain	Residue	Details
A	LEU215-ALA224

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	ACT_SITE: Proton donor => ECO:0000269|PubMed:12188666

Chain	Residue	Details
A	ASP221

---

site_id	SWS_FT_FI2
Number of Residues	1
Details	SITE: Transition state stabilizer that also modulates the pKa of Asp-245 and may act as a proton acceptor through a water chain => ECO:0000269|PubMed:2377893

Chain	Residue	Details
A	ASP175

---

site_id	SWS_FT_FI3
Number of Residues	3
Details	CARBOHYD: O-linked (Man...) threonine => ECO:0000269|PubMed:12188666, ECO:0000269|PubMed:8875646

Chain	Residue	Details
A	THR87
A	THR97
A	THR122

---

site_id	SWS_FT_FI4
Number of Residues	4
Details	CARBOHYD: O-linked (Man...) serine => ECO:0000269|PubMed:12188666, ECO:0000269|PubMed:8875646

Chain	Residue	Details
A	SER106
A	SER109
A	SER110
A	SER115

---

site_id	SWS_FT_FI5
Number of Residues	1
Details	CARBOHYD: N-linked (GlcNAc) asparagine => ECO:0000269|PubMed:12188666, ECO:0000269|PubMed:8875646

Chain	Residue	Details
A	ASN289

---

site_id	SWS_FT_FI6
Number of Residues	1
Details	CARBOHYD: N-linked (GlcNAc...) (high mannose) asparagine => ECO:0000269|PubMed:12188666, ECO:0000269|PubMed:8875646

Chain	Residue	Details
A	ASN310

---

Catalytic Information from CSA

site_id	MCSA1
Number of Residues	6
Details	M-CSA 440

Chain	Residue	Details
A	TYR169	modifies pKa, steric role
A	ARG174	electrostatic stabiliser
A	ASP175	modifies pKa, proton shuttle (general acid/base), transition state stabiliser
A	SER181	electrostatic stabiliser
A	ASP221	proton shuttle (general acid/base)
A	ASP401	electrostatic stabiliser

---