4I5U

Crystal structure of a fungal chimeric cellobiohydrolase Cel6A

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 PDB Data

site_id	AC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE ACT A 501

Chain	Residue
A	LEU283
A	ASN286
A	VAL287
A	ASN290
A	HOH690

---

site_id	AC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ACT A 502

Chain	Residue
A	VAL193
A	LYS197
A	GLU245
A	TYR249

---

site_id	AC3
Number of Residues	2
Details	BINDING SITE FOR RESIDUE EDO A 503

Chain	Residue
A	HIS414
A	HOH729

---

site_id	AC4
Number of Residues	3
Details	BINDING SITE FOR RESIDUE EDO A 504

Chain	Residue
A	ASN157
A	LYS158
A	ASP212

---

site_id	AC5
Number of Residues	4
Details	BINDING SITE FOR RESIDUE EDO A 505

Chain	Residue
A	LYS395
A	GLU399
A	EDO510
A	HOH889

---

site_id	AC6
Number of Residues	1
Details	BINDING SITE FOR RESIDUE EDO A 506

Chain	Residue
A	GLU245

---

site_id	AC7
Number of Residues	7
Details	BINDING SITE FOR RESIDUE EDO A 507

Chain	Residue
A	ASP174
A	ARG175
A	GLY184
A	TYR186
A	SER187
A	HOH853
A	HOH888

---

site_id	AC8
Number of Residues	3
Details	BINDING SITE FOR RESIDUE EDO A 508

Chain	Residue
A	PRO321
A	PRO323
A	HOH745

---

site_id	AC9
Number of Residues	3
Details	BINDING SITE FOR RESIDUE EDO A 509

Chain	Residue
A	ARG339
A	ASP344
A	LYS346

---

site_id	BC1
Number of Residues	7
Details	BINDING SITE FOR RESIDUE EDO A 510

Chain	Residue
A	TRP136
A	TYR170
A	ALA305
A	EDO505
A	HOH674
A	HOH714
A	HOH889

---

site_id	BC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE EDO A 511

Chain	Residue
A	TRP310
A	SER311
A	LYS328
A	HIS385

---

site_id	BC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE EDO A 512

Chain	Residue
A	HIS267
A	GLY365
A	HOH697
A	HOH746
A	HOH758
A	HOH793

---

site_id	BC4
Number of Residues	6
Details	BINDING SITE FOR RESIDUE PG4 A 513

Chain	Residue
A	LYS195
A	ASN198
A	VAL208
A	GLU209
A	SER211
A	HOH915

---

site_id	BC5
Number of Residues	6
Details	BINDING SITE FOR RESIDUE PGE A 514

Chain	Residue
A	LYS158
A	ASN159
A	GLN205
A	GLU209
A	HOH709
A	HOH802

---

site_id	BC6
Number of Residues	3
Details	BINDING SITE FOR RESIDUE PGE A 515

Chain	Residue
A	ARG214
A	PRO257
A	ASN258

---

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	VAL168-GLY184

---

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

Chain	Residue	Details
A	LEU216-ALA225

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	BINDING: BINDING => ECO:0000269|PubMed:10413461, ECO:0000269|PubMed:12454501, ECO:0000269|PubMed:12842048

Chain	Residue	Details
A	TRP136
A	ASP138

---

site_id	SWS_FT_FI2
Number of Residues	1
Details	CARBOHYD: O-linked (Man...) threonine => ECO:0000269|PubMed:9882628

Chain	Residue	Details
A	THR117

---

site_id	SWS_FT_FI3
Number of Residues	1
Details	CARBOHYD: O-linked (Man...) serine => ECO:0000269|PubMed:9882628

Chain	Residue	Details
A	SER126

---

site_id	SWS_FT_FI4
Number of Residues	1
Details	CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:10413461, ECO:0000269|PubMed:12454501, ECO:0000269|PubMed:12842048, ECO:0000269|PubMed:9882628

Chain	Residue	Details
A	LEU140

---

site_id	SWS_FT_FI5
Number of Residues	1
Details	ACT_SITE: Proton donor => ECO:0000269|PubMed:12188666

Chain	Residue	Details
A	ASP222

---

site_id	SWS_FT_FI6
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	ASP176

---

site_id	SWS_FT_FI7
Number of Residues	1
Details	CARBOHYD: N-linked (GlcNAc) asparagine => ECO:0000269|PubMed:12188666, ECO:0000269|PubMed:8875646

Chain	Residue	Details
A	ASN290

---

Catalytic Information from CSA

site_id	MCSA1
Number of Residues	6
Details	M-CSA 440

Chain	Residue	Details
A	TYR170	modifies pKa, steric role
A	ARG175	electrostatic stabiliser
A	ASP176	modifies pKa, proton shuttle (general acid/base), transition state stabiliser
A	SER182	electrostatic stabiliser
A	ASP222	proton shuttle (general acid/base)
A	ASP401	electrostatic stabiliser

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