eF-site ID 1auw-ABCD
PDB Code 1auw
Chain A, B, C, D

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Title H91N DELTA 2 CRYSTALLIN FROM DUCK
Classification EYE LENS PROTEIN
Compound DELTA 2 CRYSTALLIN
Source Anas platyrhynchos (Domestic duck) (Anas boschas) (CRD2_ANAPL)
Sequence A:  TDPIMEKLNSSIAYDQRLSEVDIQGSMAYAKALEKAGILT
KTELEKILSGLEKISEEWSKGVFVVKQSDEDINTANERRL
KELIGDIAGKLHTGRSRNDQVVTDLKLFMKNSLSIISTHL
LQLIKTLVERAAIEIDVILPGYTHLQKAQPIRWSQFLLSH
AVALTRDSERLGEVKKRINVLPLGSGALAGNPLDIDREML
RSELEFASISLNSMDAISERDFVVEFLSFATLLMIHLSKM
AEDLIIYSTSEFGFLTDSDAFSTGSSLMPQKKNPDSLELI
RSKAGRVFGRLASILMVLKGLPSTYNKDLQEDKEAVFDVV
DTLTAVLQVATGVISTLQISKENMEKALTPEMLATDLALY
LVRKGVPFRQAHTASGKAVHLAETKGITINKLSLEDLKSI
SPQFSSDVSQVFNFVNSVEQYTALGGTAKSSVTTQIEQLR
ELMKKQK
B:  TDPIMEKLNSSIAYDQRLSEVDIQGSMAYAKALEKAGILT
KTELEKILSGLEKISEEWSKGVFVVKQSDEDINTANERRL
KELIGDIAGKLHTGRSRNDQVVTDLKLFMKNSLSIISTHL
LQLIKTLVERAAIEIDVILPGYTHLQKAQPIRWSQFLLSH
AVALTRDSERLGEVKKRINVLPLGSGALAGNPLDIDREML
RSELEFASISLNSMDAISERDFVVEFLSFATLLMIHLSKM
AEDLIIYSTSEFGFLTDSDAFSTGSSLMPQKKNPDSLELI
RSKAGRVFGRLASILMVLKGLPSTYNKDLQEDKEAVFDVV
DTLTAVLQVATGVISTLQISKENMEKALTPEMLATDLALY
LVRKGVPFRQAHTASGKAVHLAETKGITINKLSLEDLKSI
SPQFSSDVSQVFNFVNSVEQYTALGGTAKSSVTTQIEQLR
ELMKKQK
C:  TDPIMEKLNSSIAYDQRLSEVDIQGSMAYAKALEKAGILT
KTELEKILSGLEKISEEWSKGVFVVKQSDEDINTANERRL
KELIGDIAGKLHTGRSRNDQVVTDLKLFMKNSLSIISTHL
LQLIKTLVERAAIEIDVILPGYTHLQKAQPIRWSQFLLSH
AVALTRDSERLGEVKKRINVLPLGSGALAGNPLDIDREML
RSELEFASISLNSMDAISERDFVVEFLSFATLLMIHLSKM
AEDLIIYSTSEFGFLTDSDAFSTGSSLMPQKKNPDSLELI
RSKAGRVFGRLASILMVLKGLPSTYNKDLQEDKEAVFDVV
DTLTAVLQVATGVISTLQISKENMEKALTPEMLATDLALY
LVRKGVPFRQAHTASGKAVHLAETKGITINKLSLEDLKSI
SPQFSSDVSQVFNFVNSVEQYTALGGTAKSSVTTQIEQLR
ELMKKQK
D:  TDPIMEKLNSSIAYDQRLSEVDIQGSMAYAKALEKAGILT
KTELEKILSGLEKISEEWSKGVFVVKQSDEDINTANERRL
KELIGDIAGKLHTGRSRNDQVVTDLKLFMKNSLSIISTHL
LQLIKTLVERAAIEIDVILPGYTHLQKAQPIRWSQFLLSH
AVALTRDSERLGEVKKRINVLPLGSGALAGNPLDIDREML
RSELEFASISLNSMDAISERDFVVEFLSFATLLMIHLSKM
AEDLIIYSTSEFGFLTDSDAFSTGSSLMPQKKNPDSLELI
RSKAGRVFGRLASILMVLKGLPSTYNKDLQEDKEAVFDVV
DTLTAVLQVATGVISTLQISKENMEKALTPEMLATDLALY
LVRKGVPFRQAHTASGKAVHLAETKGITINKLSLEDLKSI
SPQFSSDVSQVFNFVNSVEQYTALGGTAKSSVTTQIEQLR
ELMKKQK
Description


Functional site
1) chain A
residue 160
type
sequence H
description CATALYTIC HISTIDINE.
source : CAA
2) chain B
residue 160
type
sequence H
description CATALYTIC HISTIDINE.
source : CAB
3) chain C
residue 160
type
sequence H
description CATALYTIC HISTIDINE.
source : CAC
4) chain D
residue 160
type
sequence H
description CATALYTIC HISTIDINE.
source : CAD
5) chain A
residue 160
type catalytic
sequence H
description 408
source MCSA : MCSA1
6) chain A
residue 281
type catalytic
sequence S
description 408
source MCSA : MCSA1
7) chain A
residue 287
type catalytic
sequence K
description 408
source MCSA : MCSA1
8) chain A
residue 294
type catalytic
sequence E
description 408
source MCSA : MCSA1
9) chain B
residue 160
type catalytic
sequence H
description 408
source MCSA : MCSA2
10) chain B
residue 281
type catalytic
sequence S
description 408
source MCSA : MCSA2
11) chain B
residue 287
type catalytic
sequence K
description 408
source MCSA : MCSA2
12) chain B
residue 294
type catalytic
sequence E
description 408
source MCSA : MCSA2
13) chain C
residue 160
type catalytic
sequence H
description 408
source MCSA : MCSA3
14) chain C
residue 281
type catalytic
sequence S
description 408
source MCSA : MCSA3
15) chain C
residue 287
type catalytic
sequence K
description 408
source MCSA : MCSA3
16) chain C
residue 294
type catalytic
sequence E
description 408
source MCSA : MCSA3
17) chain D
residue 160
type catalytic
sequence H
description 408
source MCSA : MCSA4
18) chain D
residue 281
type catalytic
sequence S
description 408
source MCSA : MCSA4
19) chain D
residue 287
type catalytic
sequence K
description 408
source MCSA : MCSA4
20) chain D
residue 294
type catalytic
sequence E
description 408
source MCSA : MCSA4
21) chain A
residue 280-289
type prosite
sequence GSSLMPQKKN
description FUMARATE_LYASES Fumarate lyases signature. GSslMpQKkN
source prosite : PS00163
22) chain A
residue 160
type ACT_SITE
sequence H
description Proton acceptor => ECO:0000305|PubMed:11698398
source Swiss-Prot : SWS_FT_FI1
23) chain B
residue 160
type ACT_SITE
sequence H
description Proton acceptor => ECO:0000305|PubMed:11698398
source Swiss-Prot : SWS_FT_FI1
24) chain C
residue 160
type ACT_SITE
sequence H
description Proton acceptor => ECO:0000305|PubMed:11698398
source Swiss-Prot : SWS_FT_FI1
25) chain D
residue 160
type ACT_SITE
sequence H
description Proton acceptor => ECO:0000305|PubMed:11698398
source Swiss-Prot : SWS_FT_FI1
26) chain A
residue 281
type ACT_SITE
sequence S
description Proton donor => ECO:0000305|PubMed:11698398
source Swiss-Prot : SWS_FT_FI2
27) chain B
residue 281
type ACT_SITE
sequence S
description Proton donor => ECO:0000305|PubMed:11698398
source Swiss-Prot : SWS_FT_FI2
28) chain C
residue 281
type ACT_SITE
sequence S
description Proton donor => ECO:0000305|PubMed:11698398
source Swiss-Prot : SWS_FT_FI2
29) chain D
residue 281
type ACT_SITE
sequence S
description Proton donor => ECO:0000305|PubMed:11698398
source Swiss-Prot : SWS_FT_FI2
30) chain A
residue 27
type BINDING
sequence S
description in chain A => ECO:0000269|PubMed:11698398, ECO:0007744|PDB:1K7W
source Swiss-Prot : SWS_FT_FI3
31) chain A
residue 114
type BINDING
sequence N
description in chain A => ECO:0000269|PubMed:11698398, ECO:0007744|PDB:1K7W
source Swiss-Prot : SWS_FT_FI3
32) chain B
residue 27
type BINDING
sequence S
description in chain A => ECO:0000269|PubMed:11698398, ECO:0007744|PDB:1K7W
source Swiss-Prot : SWS_FT_FI3
33) chain B
residue 114
type BINDING
sequence N
description in chain A => ECO:0000269|PubMed:11698398, ECO:0007744|PDB:1K7W
source Swiss-Prot : SWS_FT_FI3
34) chain C
residue 27
type BINDING
sequence S
description in chain A => ECO:0000269|PubMed:11698398, ECO:0007744|PDB:1K7W
source Swiss-Prot : SWS_FT_FI3
35) chain C
residue 114
type BINDING
sequence N
description in chain A => ECO:0000269|PubMed:11698398, ECO:0007744|PDB:1K7W
source Swiss-Prot : SWS_FT_FI3
36) chain D
residue 27
type BINDING
sequence S
description in chain A => ECO:0000269|PubMed:11698398, ECO:0007744|PDB:1K7W
source Swiss-Prot : SWS_FT_FI3
37) chain D
residue 114
type BINDING
sequence N
description in chain A => ECO:0000269|PubMed:11698398, ECO:0007744|PDB:1K7W
source Swiss-Prot : SWS_FT_FI3
38) chain A
residue 159
type BINDING
sequence T
description in chain C => ECO:0000269|PubMed:10029536, ECO:0000269|PubMed:11698398, ECO:0007744|PDB:1DCN, ECO:0007744|PDB:1K7W
source Swiss-Prot : SWS_FT_FI4
39) chain B
residue 159
type BINDING
sequence T
description in chain C => ECO:0000269|PubMed:10029536, ECO:0000269|PubMed:11698398, ECO:0007744|PDB:1DCN, ECO:0007744|PDB:1K7W
source Swiss-Prot : SWS_FT_FI4
40) chain C
residue 159
type BINDING
sequence T
description in chain C => ECO:0000269|PubMed:10029536, ECO:0000269|PubMed:11698398, ECO:0007744|PDB:1DCN, ECO:0007744|PDB:1K7W
source Swiss-Prot : SWS_FT_FI4
41) chain D
residue 159
type BINDING
sequence T
description in chain C => ECO:0000269|PubMed:10029536, ECO:0000269|PubMed:11698398, ECO:0007744|PDB:1DCN, ECO:0007744|PDB:1K7W
source Swiss-Prot : SWS_FT_FI4
42) chain A
residue 289
type BINDING
sequence N
description in chain B => ECO:0000269|PubMed:10029536, ECO:0000269|PubMed:11698398, ECO:0007744|PDB:1DCN, ECO:0007744|PDB:1K7W
source Swiss-Prot : SWS_FT_FI5
43) chain B
residue 289
type BINDING
sequence N
description in chain B => ECO:0000269|PubMed:10029536, ECO:0000269|PubMed:11698398, ECO:0007744|PDB:1DCN, ECO:0007744|PDB:1K7W
source Swiss-Prot : SWS_FT_FI5
44) chain C
residue 289
type BINDING
sequence N
description in chain B => ECO:0000269|PubMed:10029536, ECO:0000269|PubMed:11698398, ECO:0007744|PDB:1DCN, ECO:0007744|PDB:1K7W
source Swiss-Prot : SWS_FT_FI5
45) chain D
residue 289
type BINDING
sequence N
description in chain B => ECO:0000269|PubMed:10029536, ECO:0000269|PubMed:11698398, ECO:0007744|PDB:1DCN, ECO:0007744|PDB:1K7W
source Swiss-Prot : SWS_FT_FI5
46) chain A
residue 321
type BINDING
sequence Y
description in chain A => ECO:0000269|PubMed:10029536, ECO:0000269|PubMed:11698398, ECO:0007744|PDB:1DCN, ECO:0007744|PDB:1K7W
source Swiss-Prot : SWS_FT_FI6
47) chain A
residue 329
type BINDING
sequence K
description in chain A => ECO:0000269|PubMed:10029536, ECO:0000269|PubMed:11698398, ECO:0007744|PDB:1DCN, ECO:0007744|PDB:1K7W
source Swiss-Prot : SWS_FT_FI6
48) chain B
residue 321
type BINDING
sequence Y
description in chain A => ECO:0000269|PubMed:10029536, ECO:0000269|PubMed:11698398, ECO:0007744|PDB:1DCN, ECO:0007744|PDB:1K7W
source Swiss-Prot : SWS_FT_FI6
49) chain B
residue 329
type BINDING
sequence K
description in chain A => ECO:0000269|PubMed:10029536, ECO:0000269|PubMed:11698398, ECO:0007744|PDB:1DCN, ECO:0007744|PDB:1K7W
source Swiss-Prot : SWS_FT_FI6
50) chain C
residue 321
type BINDING
sequence Y
description in chain A => ECO:0000269|PubMed:10029536, ECO:0000269|PubMed:11698398, ECO:0007744|PDB:1DCN, ECO:0007744|PDB:1K7W
source Swiss-Prot : SWS_FT_FI6
51) chain C
residue 329
type BINDING
sequence K
description in chain A => ECO:0000269|PubMed:10029536, ECO:0000269|PubMed:11698398, ECO:0007744|PDB:1DCN, ECO:0007744|PDB:1K7W
source Swiss-Prot : SWS_FT_FI6
52) chain D
residue 321
type BINDING
sequence Y
description in chain A => ECO:0000269|PubMed:10029536, ECO:0000269|PubMed:11698398, ECO:0007744|PDB:1DCN, ECO:0007744|PDB:1K7W
source Swiss-Prot : SWS_FT_FI6
53) chain D
residue 329
type BINDING
sequence K
description in chain A => ECO:0000269|PubMed:10029536, ECO:0000269|PubMed:11698398, ECO:0007744|PDB:1DCN, ECO:0007744|PDB:1K7W
source Swiss-Prot : SWS_FT_FI6
54) chain A
residue 326
type BINDING
sequence Q
description in chain A => ECO:0000269|PubMed:10029536, ECO:0007744|PDB:1DCN
source Swiss-Prot : SWS_FT_FI7
55) chain B
residue 326
type BINDING
sequence Q
description in chain A => ECO:0000269|PubMed:10029536, ECO:0007744|PDB:1DCN
source Swiss-Prot : SWS_FT_FI7
56) chain C
residue 326
type BINDING
sequence Q
description in chain A => ECO:0000269|PubMed:10029536, ECO:0007744|PDB:1DCN
source Swiss-Prot : SWS_FT_FI7
57) chain D
residue 326
type BINDING
sequence Q
description in chain A => ECO:0000269|PubMed:10029536, ECO:0007744|PDB:1DCN
source Swiss-Prot : SWS_FT_FI7
58) chain A
residue 294
type SITE
sequence E
description Increases basicity of active site His => ECO:0000305|PubMed:11698398
source Swiss-Prot : SWS_FT_FI8
59) chain B
residue 294
type SITE
sequence E
description Increases basicity of active site His => ECO:0000305|PubMed:11698398
source Swiss-Prot : SWS_FT_FI8
60) chain C
residue 294
type SITE
sequence E
description Increases basicity of active site His => ECO:0000305|PubMed:11698398
source Swiss-Prot : SWS_FT_FI8
61) chain D
residue 294
type SITE
sequence E
description Increases basicity of active site His => ECO:0000305|PubMed:11698398
source Swiss-Prot : SWS_FT_FI8

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