eF-site/Summary 1ocb-A

eF-site ID	1ocb-A
PDB Code	1ocb
Chain	A

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Title	Structure of the wild-type cellobiohydrolase Cel6A from Humicolas insolens in complex with a fluorescent substrate
Classification	HYDROLASE
Compound	CELLOBIOHYDROLASE II
Source	(1OCB)

Sequence	A:	NGNPFEGVQLWANNYYRSEVHTLAIPQITDPALRAAASAV AEVPSFQWLDRNVTVDTLLVQTLSEIREANQAGANPQYAA QIVVYDLPDRDCAAAASNGEWAIANNGVNNYKAYINRIRE ILISFSDVRTILVIEPDSLANMVTNMNVPKCSGAASTYRE LTIYALKQLDLPHVAMYMDAGHAGWLGWPANIQPAAELFA KIYEDAGKPRAVRGLATNVANYNAWSVSSPPPYTSPNPNY DEKHYIEAFRPLLEARGFPAQFIVDQGRSGKQPTGQKEWG HWCNAIGTGFGMRPTANTGHQYVDAFVWVKPGGECDGTSD TTAARYDYHCGLEDALKPAPEAGQWFNEYFIQLLRNANPP F

Description

Functional site


1)	chain	A
	residue	172-188
	type	prosite
	sequence	VVYDLPDRDCAAAASNG
	description	GLYCOSYL_HYDROL_F6_1 Glycosyl hydrolases family 6 signature 1. VvYdlPdRDCAaaASnG
	source	prosite : PS00655

2)	chain	A
	residue	220-229
	type	prosite
	sequence	ILVIEPDSLA
	description	GLYCOSYL_HYDROL_F6_2 Glycosyl hydrolases family 6 signature 2. ILVIEPDSLA
	source	prosite : PS00656

3)	chain	A
	residue	226
	type	ACT_SITE
	sequence	D
	description	Proton donor => ECO:0000255\|PROSITE-ProRule:PRU10057, ECO:0000269\|PubMed:10413461, ECO:0000269\|PubMed:12842048
	source	Swiss-Prot : SWS_FT_FI1

4)	chain	A
	residue	405
	type	ACT_SITE
	sequence	D
	description	Proton acceptor => ECO:0000255\|PROSITE-ProRule:PRU10056, ECO:0000269\|PubMed:10413461, ECO:0000269\|PubMed:12454501, ECO:0000269\|PubMed:12842048
	source	Swiss-Prot : SWS_FT_FI2

5)	chain	A
	residue	137
	type	BINDING
	sequence	W
	description	BINDING => ECO:0000269\|PubMed:10413461, ECO:0000269\|PubMed:12454501, ECO:0000269\|PubMed:12842048
	source	Swiss-Prot : SWS_FT_FI3

6)	chain	A
	residue	139
	type	BINDING
	sequence	D
	description	BINDING => ECO:0000269\|PubMed:10413461, ECO:0000269\|PubMed:12454501, ECO:0000269\|PubMed:12842048
	source	Swiss-Prot : SWS_FT_FI3

7)	chain	A
	residue	271
	type	BINDING
	sequence	H
	description	BINDING => ECO:0000269\|PubMed:10413461, ECO:0000269\|PubMed:12454501, ECO:0000269\|PubMed:12842048
	source	Swiss-Prot : SWS_FT_FI3

8)	chain	A
	residue	274
	type	BINDING
	sequence	W
	description	BINDING => ECO:0000269\|PubMed:10413461, ECO:0000269\|PubMed:12454501, ECO:0000269\|PubMed:12842048
	source	Swiss-Prot : SWS_FT_FI3

9)	chain	A
	residue	310
	type	BINDING
	sequence	N
	description	BINDING => ECO:0000269\|PubMed:10413461, ECO:0000269\|PubMed:12454501, ECO:0000269\|PubMed:12842048
	source	Swiss-Prot : SWS_FT_FI3

10)	chain	A
	residue	371
	type	BINDING
	sequence	W
	description	BINDING => ECO:0000269\|PubMed:10413461, ECO:0000269\|PubMed:12454501, ECO:0000269\|PubMed:12842048
	source	Swiss-Prot : SWS_FT_FI3

11)	chain	A
	residue	399
	type	BINDING
	sequence	K
	description	BINDING => ECO:0000269\|PubMed:10413461, ECO:0000269\|PubMed:12454501, ECO:0000269\|PubMed:12842048
	source	Swiss-Prot : SWS_FT_FI3

12)	chain	A
	residue	403
	type	BINDING
	sequence	E
	description	BINDING => ECO:0000269\|PubMed:10413461, ECO:0000269\|PubMed:12454501, ECO:0000269\|PubMed:12842048
	source	Swiss-Prot : SWS_FT_FI3

13)	chain	A
	residue	118
	type	CARBOHYD
	sequence	T
	description	O-linked (Man...) threonine => ECO:0000269\|PubMed:9882628
	source	Swiss-Prot : SWS_FT_FI4

14)	chain	A
	residue	127
	type	CARBOHYD
	sequence	S
	description	O-linked (Man...) serine => ECO:0000269\|PubMed:9882628
	source	Swiss-Prot : SWS_FT_FI5

15)	chain	A
	residue	141
	type	CARBOHYD
	sequence	N
	description	N-linked (GlcNAc...) asparagine => ECO:0000269\|PubMed:10413461, ECO:0000269\|PubMed:12454501, ECO:0000269\|PubMed:12842048, ECO:0000269\|PubMed:9882628
	source	Swiss-Prot : SWS_FT_FI6