eF-site ID 4ax7-ABCD
PDB Code 4ax7
Chain A, B, C, D

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Title Hypocrea jecorina Cel6A D221A mutant soaked with 4-Methylumbelliferyl- beta-D-cellobioside
Classification HYDROLASE
Compound EXOGLUCANASE 2
Source (GUX2_HYPJE)
Sequence A:  TATYSGNPFVGVTPWANAYYASEVSSLAIPSLTGAMATAA
AAVAKVPSFMWLDTLDKTPLMEQTLADIRTANKNGGNYAG
QFVVYDLPDRDCAALASNGEYSIADGGVAKYKNYIDTIRQ
IVVEYSDIRTLLVIEPASLANLVTNLGTPKCANAQSAYLE
CINYAVTQLNLPNVAMYLDAGHAGWLGWPANQDPAAQLFA
NVYKNASSPRALRGLATNVANYNGWNITSPPSYTQGNAVY
NEKLYIHAIGPLLANHGWSNAFFITDQGRSGKQPTGQQQW
GDWCNVIGTGFGIRPSANTGDSLLDSFVWVKPGGECDGTS
DSSAPRFDSHCALPDALQPAPQAGAWFQAYFVQLLTNANP
SFL
B:  TATYSGNPFVGVTPWANAYYASEVSSLAIPSLTGAMATAA
AAVAKVPSFMWLDTLDKTPLMEQTLADIRTANKNGGNYAG
QFVVYDLPDRDCAANGEYSIADGGVAKYKNYIDTIRQIVV
EYSDIRTLLVIEPASLANLVTNLGTPKCANAQSAYLECIN
YAVTQLNLPNVAMYLDAGHAGWLGWPANQDPAAQLFANVY
KNASSPRALRGLATNVANYNGWNITSPPSYTQGNAVYNEK
LYIHAIGPLLANHGWSNAFFITDQGRSGKQPTGQQQWGDW
CNVIGTGFGIRPSANTGDSLLDSFVWVKPGGECDGTSDSS
APRFDSHCALPDALQPAPQAGAWFQAYFVQLLTNANPSFL
C:  TATYSGNPFVGVTPWANAYYASEVSSLAIPSLTGAMATAA
AAVAKVPSFMWLDTLDKTPLMEQTLADIRTANKNGGNYAG
QFVVYDLPDRDCAALASNGEYSIADGGVAKYKNYIDTIRQ
IVVEYSDIRTLLVIEPASLANLVTNLGTPKCANAQSAYLE
CINYAVTQLNLPNVAMYLDAGHAGWLGWPANQDPAAQLFA
NVYKNASSPRALRGLATNVANYNGWNITSPPSYTQGNAVY
NEKLYIHAIGPLLANHGWSNAFFITDQGRSGKQPTGQQQW
GDWCNVIGTGFGIRPSANTGDSLLDSFVWVKPGGECDGTS
DSSAPRFDSHCALPDALQPAPQAGAWFQAYFVQLLTNANP
SFL
D:  TATYSGNPFVGVTPWANAYYASEVSSLAIPSLTGAMATAA
AAVAKVPSFMWLDTLDKTPLMEQTLADIRTANKNGGNYAG
QFVVYDLPDRDCAANGEYSIADGGVAKYKNYIDTIRQIVV
EYSDIRTLLVIEPASLANLVTNLGTPKCANAQSAYLECIN
YAVTQLNLPNVAMYLDAGHAGWLGWPANQDPAAQLFANVY
KNASSPRALRGLATNVANYNGWNITSPPSYTQGNAVYNEK
LYIHAIGPLLANHGWSNAFFITDQGRSGKQPTGQQQWGDW
CNVIGTGFGIRPSANTGDSLLDSFVWVKPGGECDGTSDSS
APRFDSHCALPDALQPAPQAGAWFQAYFVQLLTNANPSFL
Description


Functional site
1) chain A
residue 169
type catalytic
sequence Y
description 440
source MCSA : MCSA1
2) chain A
residue 174
type catalytic
sequence R
description 440
source MCSA : MCSA1
3) chain A
residue 175
type catalytic
sequence D
description 440
source MCSA : MCSA1
4) chain A
residue 181
type catalytic
sequence S
description 440
source MCSA : MCSA1
5) chain A
residue 221
type catalytic
sequence A
description 440
source MCSA : MCSA1
6) chain A
residue 401
type catalytic
sequence D
description 440
source MCSA : MCSA1
7) chain B
residue 169
type catalytic
sequence Y
description 440
source MCSA : MCSA2
8) chain B
residue 174
type catalytic
sequence R
description 440
source MCSA : MCSA2
9) chain B
residue 175
type catalytic
sequence D
description 440
source MCSA : MCSA2
10) chain B
residue 221
type catalytic
sequence A
description 440
source MCSA : MCSA2
11) chain B
residue 401
type catalytic
sequence D
description 440
source MCSA : MCSA2
12) chain C
residue 169
type catalytic
sequence Y
description 440
source MCSA : MCSA3
13) chain C
residue 174
type catalytic
sequence R
description 440
source MCSA : MCSA3
14) chain C
residue 175
type catalytic
sequence D
description 440
source MCSA : MCSA3
15) chain C
residue 181
type catalytic
sequence S
description 440
source MCSA : MCSA3
16) chain C
residue 221
type catalytic
sequence A
description 440
source MCSA : MCSA3
17) chain C
residue 401
type catalytic
sequence D
description 440
source MCSA : MCSA3
18) chain D
residue 169
type catalytic
sequence Y
description 440
source MCSA : MCSA4
19) chain D
residue 174
type catalytic
sequence R
description 440
source MCSA : MCSA4
20) chain D
residue 175
type catalytic
sequence D
description 440
source MCSA : MCSA4
21) chain D
residue 221
type catalytic
sequence A
description 440
source MCSA : MCSA4
22) chain D
residue 401
type catalytic
sequence D
description 440
source MCSA : MCSA4
23) chain A
residue 221
type ACT_SITE
sequence A
description Proton donor => ECO:0000269|PubMed:12188666
source Swiss-Prot : SWS_FT_FI1
24) chain B
residue 221
type ACT_SITE
sequence A
description Proton donor => ECO:0000269|PubMed:12188666
source Swiss-Prot : SWS_FT_FI1
25) chain C
residue 221
type ACT_SITE
sequence A
description Proton donor => ECO:0000269|PubMed:12188666
source Swiss-Prot : SWS_FT_FI1
26) chain D
residue 221
type ACT_SITE
sequence A
description Proton donor => ECO:0000269|PubMed:12188666
source Swiss-Prot : SWS_FT_FI1
27) chain A
residue 175
type SITE
sequence D
description 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
source Swiss-Prot : SWS_FT_FI2
28) chain B
residue 175
type SITE
sequence D
description 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
source Swiss-Prot : SWS_FT_FI2
29) chain C
residue 175
type SITE
sequence D
description 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
source Swiss-Prot : SWS_FT_FI2
30) chain D
residue 175
type SITE
sequence D
description 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
source Swiss-Prot : SWS_FT_FI2
31) chain A
residue 87
type CARBOHYD
sequence T
description O-linked (Man...) threonine => ECO:0000269|PubMed:12188666, ECO:0000269|PubMed:8875646
source Swiss-Prot : SWS_FT_FI3
32) chain D
residue 87
type CARBOHYD
sequence T
description O-linked (Man...) threonine => ECO:0000269|PubMed:12188666, ECO:0000269|PubMed:8875646
source Swiss-Prot : SWS_FT_FI3
33) chain D
residue 97
type CARBOHYD
sequence T
description O-linked (Man...) threonine => ECO:0000269|PubMed:12188666, ECO:0000269|PubMed:8875646
source Swiss-Prot : SWS_FT_FI3
34) chain D
residue 122
type CARBOHYD
sequence T
description O-linked (Man...) threonine => ECO:0000269|PubMed:12188666, ECO:0000269|PubMed:8875646
source Swiss-Prot : SWS_FT_FI3
35) chain A
residue 97
type CARBOHYD
sequence T
description O-linked (Man...) threonine => ECO:0000269|PubMed:12188666, ECO:0000269|PubMed:8875646
source Swiss-Prot : SWS_FT_FI3
36) chain A
residue 122
type CARBOHYD
sequence T
description O-linked (Man...) threonine => ECO:0000269|PubMed:12188666, ECO:0000269|PubMed:8875646
source Swiss-Prot : SWS_FT_FI3
37) chain B
residue 87
type CARBOHYD
sequence T
description O-linked (Man...) threonine => ECO:0000269|PubMed:12188666, ECO:0000269|PubMed:8875646
source Swiss-Prot : SWS_FT_FI3
38) chain B
residue 97
type CARBOHYD
sequence T
description O-linked (Man...) threonine => ECO:0000269|PubMed:12188666, ECO:0000269|PubMed:8875646
source Swiss-Prot : SWS_FT_FI3
39) chain B
residue 122
type CARBOHYD
sequence T
description O-linked (Man...) threonine => ECO:0000269|PubMed:12188666, ECO:0000269|PubMed:8875646
source Swiss-Prot : SWS_FT_FI3
40) chain C
residue 87
type CARBOHYD
sequence T
description O-linked (Man...) threonine => ECO:0000269|PubMed:12188666, ECO:0000269|PubMed:8875646
source Swiss-Prot : SWS_FT_FI3
41) chain C
residue 97
type CARBOHYD
sequence T
description O-linked (Man...) threonine => ECO:0000269|PubMed:12188666, ECO:0000269|PubMed:8875646
source Swiss-Prot : SWS_FT_FI3
42) chain C
residue 122
type CARBOHYD
sequence T
description O-linked (Man...) threonine => ECO:0000269|PubMed:12188666, ECO:0000269|PubMed:8875646
source Swiss-Prot : SWS_FT_FI3
43) chain A
residue 106
type CARBOHYD
sequence S
description O-linked (Man...) serine => ECO:0000269|PubMed:12188666, ECO:0000269|PubMed:8875646
source Swiss-Prot : SWS_FT_FI4
44) chain C
residue 109
type CARBOHYD
sequence S
description O-linked (Man...) serine => ECO:0000269|PubMed:12188666, ECO:0000269|PubMed:8875646
source Swiss-Prot : SWS_FT_FI4
45) chain C
residue 110
type CARBOHYD
sequence S
description O-linked (Man...) serine => ECO:0000269|PubMed:12188666, ECO:0000269|PubMed:8875646
source Swiss-Prot : SWS_FT_FI4
46) chain C
residue 115
type CARBOHYD
sequence S
description O-linked (Man...) serine => ECO:0000269|PubMed:12188666, ECO:0000269|PubMed:8875646
source Swiss-Prot : SWS_FT_FI4
47) chain D
residue 106
type CARBOHYD
sequence S
description O-linked (Man...) serine => ECO:0000269|PubMed:12188666, ECO:0000269|PubMed:8875646
source Swiss-Prot : SWS_FT_FI4
48) chain D
residue 109
type CARBOHYD
sequence S
description O-linked (Man...) serine => ECO:0000269|PubMed:12188666, ECO:0000269|PubMed:8875646
source Swiss-Prot : SWS_FT_FI4
49) chain D
residue 110
type CARBOHYD
sequence S
description O-linked (Man...) serine => ECO:0000269|PubMed:12188666, ECO:0000269|PubMed:8875646
source Swiss-Prot : SWS_FT_FI4
50) chain D
residue 115
type CARBOHYD
sequence S
description O-linked (Man...) serine => ECO:0000269|PubMed:12188666, ECO:0000269|PubMed:8875646
source Swiss-Prot : SWS_FT_FI4
51) chain A
residue 109
type CARBOHYD
sequence S
description O-linked (Man...) serine => ECO:0000269|PubMed:12188666, ECO:0000269|PubMed:8875646
source Swiss-Prot : SWS_FT_FI4
52) chain A
residue 110
type CARBOHYD
sequence S
description O-linked (Man...) serine => ECO:0000269|PubMed:12188666, ECO:0000269|PubMed:8875646
source Swiss-Prot : SWS_FT_FI4
53) chain A
residue 115
type CARBOHYD
sequence S
description O-linked (Man...) serine => ECO:0000269|PubMed:12188666, ECO:0000269|PubMed:8875646
source Swiss-Prot : SWS_FT_FI4
54) chain B
residue 106
type CARBOHYD
sequence S
description O-linked (Man...) serine => ECO:0000269|PubMed:12188666, ECO:0000269|PubMed:8875646
source Swiss-Prot : SWS_FT_FI4
55) chain B
residue 109
type CARBOHYD
sequence S
description O-linked (Man...) serine => ECO:0000269|PubMed:12188666, ECO:0000269|PubMed:8875646
source Swiss-Prot : SWS_FT_FI4
56) chain B
residue 110
type CARBOHYD
sequence S
description O-linked (Man...) serine => ECO:0000269|PubMed:12188666, ECO:0000269|PubMed:8875646
source Swiss-Prot : SWS_FT_FI4
57) chain B
residue 115
type CARBOHYD
sequence S
description O-linked (Man...) serine => ECO:0000269|PubMed:12188666, ECO:0000269|PubMed:8875646
source Swiss-Prot : SWS_FT_FI4
58) chain C
residue 106
type CARBOHYD
sequence S
description O-linked (Man...) serine => ECO:0000269|PubMed:12188666, ECO:0000269|PubMed:8875646
source Swiss-Prot : SWS_FT_FI4
59) chain A
residue 289
type CARBOHYD
sequence N
description N-linked (GlcNAc) asparagine => ECO:0000269|PubMed:12188666, ECO:0000269|PubMed:8875646
source Swiss-Prot : SWS_FT_FI5
60) chain B
residue 289
type CARBOHYD
sequence N
description N-linked (GlcNAc) asparagine => ECO:0000269|PubMed:12188666, ECO:0000269|PubMed:8875646
source Swiss-Prot : SWS_FT_FI5
61) chain C
residue 289
type CARBOHYD
sequence N
description N-linked (GlcNAc) asparagine => ECO:0000269|PubMed:12188666, ECO:0000269|PubMed:8875646
source Swiss-Prot : SWS_FT_FI5
62) chain D
residue 289
type CARBOHYD
sequence N
description N-linked (GlcNAc) asparagine => ECO:0000269|PubMed:12188666, ECO:0000269|PubMed:8875646
source Swiss-Prot : SWS_FT_FI5
63) chain A
residue 310
type CARBOHYD
sequence N
description N-linked (GlcNAc...) (high mannose) asparagine => ECO:0000269|PubMed:12188666, ECO:0000269|PubMed:8875646
source Swiss-Prot : SWS_FT_FI6
64) chain B
residue 310
type CARBOHYD
sequence N
description N-linked (GlcNAc...) (high mannose) asparagine => ECO:0000269|PubMed:12188666, ECO:0000269|PubMed:8875646
source Swiss-Prot : SWS_FT_FI6
65) chain C
residue 310
type CARBOHYD
sequence N
description N-linked (GlcNAc...) (high mannose) asparagine => ECO:0000269|PubMed:12188666, ECO:0000269|PubMed:8875646
source Swiss-Prot : SWS_FT_FI6
66) chain D
residue 310
type CARBOHYD
sequence N
description N-linked (GlcNAc...) (high mannose) asparagine => ECO:0000269|PubMed:12188666, ECO:0000269|PubMed:8875646
source Swiss-Prot : SWS_FT_FI6
67) chain A
residue 167-183
type prosite
sequence VVYDLPDRDCAALASNG
description GLYCOSYL_HYDROL_F6_1 Glycosyl hydrolases family 6 signature 1. VvYdlPdRDCAalASnG
source prosite : PS00655

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