eF-site ID 6sxs-.AAA
PDB Code 6sxs
Chain AAA

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Title GH54 a-l-arabinofuranosidase soaked with cyclic sulfate inhibitor
Classification HYDROLASE
Compound Alpha-L-arabinofuranosidase B
Source (ABFB_ASPKW)
Sequence AAA:  MGPCDIYEAGDTPCVAAHSTTRALYSSFSGALYQLQRGSD
DTTTTISPLTAGGIADASAQDTFCANTTCLITIIYDQSGN
GNHLTQAPPGGFDGPDTDGYDNLASAIGAPVTLNGQKAYG
VFMSPGTGYRNNEATGTATGDEAEGMYAVLDGTHYNDACC
FDYGNAETSSTDTGAGHMEAIYLGNSTTWGYGAGDGPWIM
VDMENNLFSGADEGYNSGDPSISYRFVTAAVKGGADKWAI
RGANAASGSLSTYYSGARPDYSGYNPMSKEGAIILGIGGD
NSNGAQGTFYEGVMTSGYPSDDTENSVQENIVAAKYVVGS
LVSGPSFTSGEVVSLRVTTPGYTTRYIAHTDTTVNTQVVD
DDSSTTLKEEASWTVVTGLANSQCFSFESVDTPGSYIRHY
NFELLLNANDGTKQFHEDATFCPQAALNGEGTSLRSWSYP
TRYFRHYENVLYAASNGGVQTFDSKTSFNNDVSFEIETAF
A
Description


Functional site

1) chain AAA
residue 176
type SITE
sequence C
description Cis-peptide bond => ECO:0000269|PubMed:15292273
source Swiss-Prot : SWS_FT_FI4

2) chain AAA
residue 83
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000255
source Swiss-Prot : SWS_FT_FI5

3) chain AAA
residue 202
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:15292273
source Swiss-Prot : SWS_FT_FI6

4) chain AAA
residue 221
type ACT_SITE
sequence E
description Nucleophile => ECO:0000269|PubMed:15292273
source Swiss-Prot : SWS_FT_FI1

5) chain AAA
residue 297
type ACT_SITE
sequence D
description Proton donor => ECO:0000269|PubMed:15292273
source Swiss-Prot : SWS_FT_FI2

6) chain AAA
residue 465
type BINDING
sequence E
description BINDING => ECO:0000269|PubMed:15292273, ECO:0000269|PubMed:16846393
source Swiss-Prot : SWS_FT_FI3

7) chain AAA
residue 468
type BINDING
sequence L
description BINDING => ECO:0000269|PubMed:15292273, ECO:0000269|PubMed:16846393
source Swiss-Prot : SWS_FT_FI3

8) chain AAA
residue 488
type BINDING
sequence D
description BINDING => ECO:0000269|PubMed:15292273, ECO:0000269|PubMed:16846393
source Swiss-Prot : SWS_FT_FI3

9) chain AAA
residue 418
type BINDING
sequence N
description BINDING => ECO:0000269|PubMed:15292273, ECO:0000269|PubMed:16846393
source Swiss-Prot : SWS_FT_FI3

10) chain AAA
residue 419
type BINDING
sequence F
description BINDING => ECO:0000269|PubMed:15292273, ECO:0000269|PubMed:16846393
source Swiss-Prot : SWS_FT_FI3

11) chain AAA
residue 435
type BINDING
sequence D
description BINDING => ECO:0000269|PubMed:15292273, ECO:0000269|PubMed:16846393
source Swiss-Prot : SWS_FT_FI3

12) chain AAA
residue 463
type BINDING
sequence H
description BINDING => ECO:0000269|PubMed:15292273, ECO:0000269|PubMed:16846393
source Swiss-Prot : SWS_FT_FI3

13) chain AAA
residue 222
type BINDING
sequence N
description BINDING => ECO:0000269|PubMed:15292273, ECO:0000269|PubMed:16846393
source Swiss-Prot : SWS_FT_FI3

14) chain AAA
residue 223
type BINDING
sequence N
description BINDING => ECO:0000269|PubMed:15292273, ECO:0000269|PubMed:16846393
source Swiss-Prot : SWS_FT_FI3

15) chain AAA
residue 296
type BINDING
sequence G
description BINDING => ECO:0000269|PubMed:15292273, ECO:0000269|PubMed:16846393
source Swiss-Prot : SWS_FT_FI3

16) chain AAA
residue 416
type BINDING
sequence H
description BINDING => ECO:0000269|PubMed:15292273, ECO:0000269|PubMed:16846393
source Swiss-Prot : SWS_FT_FI3

17) chain AAA
residue 219
type BINDING
sequence D
description BINDING => ECO:0000269|PubMed:15292273, ECO:0000269|PubMed:16846393
source Swiss-Prot : SWS_FT_FI3


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