eF-site ID 6c4j-A
PDB Code 6c4j
Chain A

click to enlarge
Title Ligand bound full length hUGDH with A104L substitution
Classification OXIDOREDUCTASE
Compound UDP-glucose 6-dehydrogenase
Source (UGDH_HUMAN)
Sequence A:  FEIKKICCIGAGYVGGPTCSVIRVTVEPGLKEVVESCRGK
NLSTNIDDAIKELVFISVNTPTKTYGMGKGRALDLKYIEA
CARRIVQNSNGYKIVTEKSTVPVRAAESIRRIFDANTKPN
LQVLSNPEFLAEGTAIKDLKNPDRVLIGGDETPEGQRAVQ
ALCAVYEHWVPREKILTTNTWSSELSKLAANAFLAQRISS
INSISALCEATGADVEEVATAIGMDQRIGNKFLKASVGFG
GSCFQKDVLNLVYLCEALNLPEVARYWQQVIDMNDYQRRR
FASRIIDSLFNTVTDKKIAILGFAFKKDTGDTRESSSIYI
SKYLMDEGAHLHIYDPKVPREQIVVDLSHQVSRLVTISKD
PYEACDGAHAVVICTEWDMFKELDYERIHKKMLKPAFIFD
GRRVLDGLHNELQTIGFQIETIGKKV
Description


Functional site
1) chain A
residue 13
type
sequence G
description binding site for residue NAD A 501
source : AC1
2) chain A
residue 14
type
sequence Y
description binding site for residue NAD A 501
source : AC1
3) chain A
residue 15
type
sequence V
description binding site for residue NAD A 501
source : AC1
4) chain A
residue 89
type
sequence V
description binding site for residue NAD A 501
source : AC1
5) chain A
residue 90
type
sequence N
description binding site for residue NAD A 501
source : AC1
6) chain A
residue 91
type
sequence T
description binding site for residue NAD A 501
source : AC1
7) chain A
residue 108
type
sequence Y
description binding site for residue NAD A 501
source : AC1
8) chain A
residue 112
type
sequence C
description binding site for residue NAD A 501
source : AC1
9) chain A
residue 131
type
sequence T
description binding site for residue NAD A 501
source : AC1
10) chain A
residue 161
type
sequence E
description binding site for residue NAD A 501
source : AC1
11) chain A
residue 276
type
sequence C
description binding site for residue NAD A 501
source : AC1
12) chain A
residue 279
type
sequence K
description binding site for residue NAD A 501
source : AC1
13) chain A
residue 162
type
sequence F
description binding site for residue UPG A 502
source : AC2
14) chain A
residue 163
type
sequence L
description binding site for residue UPG A 502
source : AC2
15) chain A
residue 164
type
sequence A
description binding site for residue UPG A 502
source : AC2
16) chain A
residue 165
type
sequence E
description binding site for residue UPG A 502
source : AC2
17) chain A
residue 220
type
sequence K
description binding site for residue UPG A 502
source : AC2
18) chain A
residue 224
type
sequence N
description binding site for residue UPG A 502
source : AC2
19) chain A
residue 231
type
sequence I
description binding site for residue UPG A 502
source : AC2
20) chain A
residue 265
type
sequence F
description binding site for residue UPG A 502
source : AC2
21) chain A
residue 266
type
sequence L
description binding site for residue UPG A 502
source : AC2
22) chain A
residue 267
type
sequence K
description binding site for residue UPG A 502
source : AC2
23) chain A
residue 269
type
sequence S
description binding site for residue UPG A 502
source : AC2
24) chain A
residue 272
type
sequence F
description binding site for residue UPG A 502
source : AC2
25) chain A
residue 273
type
sequence G
description binding site for residue UPG A 502
source : AC2
26) chain A
residue 276
type
sequence C
description binding site for residue UPG A 502
source : AC2
27) chain A
residue 277
type
sequence F
description binding site for residue UPG A 502
source : AC2
28) chain A
residue 338
type
sequence F
description binding site for residue UPG A 502
source : AC2
29) chain A
residue 339
type
sequence K
description binding site for residue UPG A 502
source : AC2
30) chain A
residue 442
type
sequence R
description binding site for residue UPG A 502
source : AC2
31) chain A
residue 135
type
sequence R
description binding site for residue CL A 503
source : AC3
32) chain A
residue 214
type
sequence W
description binding site for residue CL A 503
source : AC3
33) chain A
residue 260
type
sequence R
description binding site for residue UPG B 502
source : AC5
34) chain A
residue 161
type ACT_SITE
sequence E
description Proton donor/acceptor => ECO:0000269|PubMed:22123821
source Swiss-Prot : SWS_FT_FI1
35) chain A
residue 220
type ACT_SITE
sequence K
description Proton donor/acceptor => ECO:0000269|PubMed:22123821
source Swiss-Prot : SWS_FT_FI1
36) chain A
residue 276
type ACT_SITE
sequence C
description Nucleophile => ECO:0000269|PubMed:21502315, ECO:0000269|PubMed:21984906, ECO:0000269|PubMed:22123821
source Swiss-Prot : SWS_FT_FI2
37) chain A
residue 11
type BINDING
sequence G
description BINDING => ECO:0000269|PubMed:21502315, ECO:0000269|PubMed:21595445, ECO:0000269|PubMed:21984906, ECO:0007744|PDB:2Q3E, ECO:0007744|PDB:2QG4, ECO:0007744|PDB:3PRJ, ECO:0007744|PDB:3PTZ, ECO:0007744|PDB:3TDK
source Swiss-Prot : SWS_FT_FI3
38) chain A
residue 89
type BINDING
sequence V
description BINDING => ECO:0000269|PubMed:21502315, ECO:0000269|PubMed:21595445, ECO:0000269|PubMed:21984906, ECO:0007744|PDB:2Q3E, ECO:0007744|PDB:2QG4, ECO:0007744|PDB:3PRJ, ECO:0007744|PDB:3PTZ, ECO:0007744|PDB:3TDK
source Swiss-Prot : SWS_FT_FI3
39) chain A
residue 276
type BINDING
sequence C
description BINDING => ECO:0000269|PubMed:21502315, ECO:0000269|PubMed:21595445, ECO:0000269|PubMed:21984906, ECO:0007744|PDB:2Q3E, ECO:0007744|PDB:2QG4, ECO:0007744|PDB:3PRJ, ECO:0007744|PDB:3PTZ, ECO:0007744|PDB:3TDK
source Swiss-Prot : SWS_FT_FI3
40) chain A
residue 130
type BINDING
sequence S
description BINDING => ECO:0000269|PubMed:21502315, ECO:0000269|PubMed:21595445
source Swiss-Prot : SWS_FT_FI4
41) chain A
residue 161
type BINDING
sequence E
description BINDING => ECO:0000269|PubMed:23106432, ECO:0000305|PubMed:21502315, ECO:0000305|PubMed:21595445, ECO:0007744|PDB:2QG4, ECO:0007744|PDB:3PRJ, ECO:0007744|PDB:3PTZ, ECO:0007744|PDB:4EDF
source Swiss-Prot : SWS_FT_FI5
42) chain A
residue 220
type BINDING
sequence K
description BINDING => ECO:0000269|PubMed:23106432, ECO:0000305|PubMed:21502315, ECO:0000305|PubMed:21595445, ECO:0007744|PDB:2QG4, ECO:0007744|PDB:3PRJ, ECO:0007744|PDB:3PTZ, ECO:0007744|PDB:4EDF
source Swiss-Prot : SWS_FT_FI5
43) chain A
residue 267
type BINDING
sequence K
description BINDING => ECO:0000269|PubMed:23106432, ECO:0000305|PubMed:21502315, ECO:0000305|PubMed:21595445, ECO:0007744|PDB:2QG4, ECO:0007744|PDB:3PRJ, ECO:0007744|PDB:3PTZ, ECO:0007744|PDB:4EDF
source Swiss-Prot : SWS_FT_FI5
44) chain A
residue 338
type BINDING
sequence F
description BINDING => ECO:0000269|PubMed:23106432, ECO:0000305|PubMed:21502315, ECO:0000305|PubMed:21595445, ECO:0007744|PDB:2QG4, ECO:0007744|PDB:3PRJ, ECO:0007744|PDB:3PTZ, ECO:0007744|PDB:4EDF
source Swiss-Prot : SWS_FT_FI5
45) chain A
residue 165
type BINDING
sequence E
description BINDING => ECO:0000269|PubMed:21502315, ECO:0007744|PDB:2Q3E, ECO:0007744|PDB:2QG4
source Swiss-Prot : SWS_FT_FI6
46) chain A
residue 107
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0007744|PubMed:19608861
source Swiss-Prot : SWS_FT_FI10
47) chain A
residue 260
type BINDING
sequence R
description BINDING => ECO:0000269|PubMed:23106432, ECO:0000269|PubMed:27966912, ECO:0000305|PubMed:21502315, ECO:0000305|PubMed:21595445, ECO:0007744|PDB:2QG4, ECO:0007744|PDB:3PRJ, ECO:0007744|PDB:3PTZ, ECO:0007744|PDB:4EDF, ECO:0007744|PDB:5TJH
source Swiss-Prot : SWS_FT_FI7
48) chain A
residue 346
type BINDING
sequence R
description BINDING => ECO:0000269|PubMed:21502315, ECO:0000269|PubMed:21595445, ECO:0000269|PubMed:21984906, ECO:0000269|PubMed:22123821, ECO:0007744|PDB:2Q3E, ECO:0007744|PDB:2QG4, ECO:0007744|PDB:3PRJ, ECO:0007744|PDB:3PTZ, ECO:0007744|PDB:3TDK
source Swiss-Prot : SWS_FT_FI8
49) chain A
residue 442
type BINDING
sequence R
description BINDING => ECO:0000269|PubMed:22123821, ECO:0000269|PubMed:23106432, ECO:0000305|PubMed:21502315, ECO:0000305|PubMed:21595445, ECO:0007744|PDB:2QG4, ECO:0007744|PDB:3KHU, ECO:0007744|PDB:3PRJ, ECO:0007744|PDB:3PTZ, ECO:0007744|PDB:4EDF
source Swiss-Prot : SWS_FT_FI9

Display surface

Download
Links