eF-site ID 5e6s-ABCDEF
PDB Code 5e6s
Chain A, B, C, D, E, F

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Title Structures of leukocyte integrin aLB2: The aI domain, the headpiece, and the pocket for the internal ligand
Classification CELL ADHESION
Compound Integrin alpha-L
Source (ITB2_HUMAN)
Sequence A:  YNLDVRGARSFSPPRAGRHFGYRVLQVGNGVIVGAPGEGN
STGSLYQCQSGTGHCLPVTLRGSNYTSKYLGMTLATDPTD
GSILACDPGLSRTCDQNTYLSGLCYLFRQNLQGPMLQGRP
GFQECIKGNVDLVFLFDGSMSLQPDEFQKILDFMKDVMKK
LSNTSYQFAAVQFSTSYKTEFDFSDYVKWKDPDALLKHVK
HMLLLTNTFGAINYVATEVFREELGARPDATKVLIIITDG
EATDSGNIDAAKDIIRYIIGIGKHFQTKESQETLHKFASK
PASEFVKILDTFEKLKDLFTELQKKILTSFNMELSSSGIS
ADLSRGHAVVGAVGAKDWAGGFLDLKADLQDDTFIGNEPL
TPEVRAGYLGYTVTWLPSRQKTSLLASGAPRYQHMGRVLL
FQEPQGGGHWSQVQTIHGTQIGSYFGGELCGVDVDQDGET
ELLLIGAPLFYGEQRGGRVFIYQRRQLGFEEVSELQGDPG
YPLGRFGEAITALTDINGDGLVDVAVGAPLEEQGAVYIFN
GRHGGLSPQPSQRIEGTQVLSGIQWFGRSIHGVKDLEGDG
LADVAVGAESQMIVLSSRP
B:  QECTKFKVSSCRECIESGPGCTWCQKLNFTGPGDPDSIRC
DTRPQLLMRGCAADDIMDPTSLAETQEDQKQLSPQKVTLY
LRPGQAAAFNVTFRRAKGYPIDLYYLMDLSYSMLDDLRNV
KKLGGDLLRALNEITESGRIGFGSFVDKTVLPFVNTHPDK
LRNPCPNKEKECQPPFAFRHVLKLTNNSNQFQTEVGKQLI
SGNLDAPEGGLDAMMQVAACPEEIGWRKVTRLLVFATDDG
FHFAGDGKLGAILTPNDGRCHLEDNLYKRSNEFDYPSVGQ
LAHKLAENNIQPIFAVTSRMVKTYEKLTEIIPKSAVGELS
EDSSNVVQLIKNAYNKLSSRVFLDHNALPDTLKVTYDSFC
SNGVTHRNQPRGDCDGVQINVPITFQVKVTATECIQEQSF
VIRALGFTDIVTVQVLPQCECRCRDQSRDRSLCHGKGFLE
CGICRCDTGYIGKNC
C:  YNLDVRGARSFSPPRAGRHFGYRVLQVGNGVIVGAPGEGN
STGSLYQCQSGTGHCLPVTLRGSNYTSKYLGMTLATDPTD
GSILACDPGLSRTCDQNTYLSGLCYLFRQNLQGPMLQGRP
GFQECIKGNVDLVFLFDGSMSLQPDEFQKILDFMKDVMKK
LSNTSYQFAAVQFSTSYKTEFDFSDYVKWKDPDALLKHVK
HMLLLTNTFGAINYVATEVFREELGARPDATKVLIIITDG
EATDSGNIDAAKDIIRYIIGIGKHFQTKESQETLHKFASK
PASEFVKILDTFEKLKDLFTELQKLTSFNMELSSSGISAD
LSRGHAVVGAVGAKDWAGGFLDLKADLQDDTFIGNEPLTP
EVRAGYLGYTVTWLPSRQKTSLLASGAPRYQHMGRVLLFQ
EPQGGGHWSQVQTIHGTQIGSYFGGELCGVDVDQDGETEL
LLIGAPLFYGEQRGGRVFIYQRRQLGFEEVSELQGDPGYP
LGRFGEAITALTDINGDGLVDVAVGAPLEEQGAVYIFNGR
HGGLSPQPSQRIEGTQVLSGIQWFGRSIHGVKDLEGDGLA
DVAVGAESQMIVLSSRPV
D:  QECTKFKVSSCRECIESGPGCTWCQKLNFTGPGDPDSIRC
DTRPQLLMRGCAADDIMDPTSLAETQEDQKQLSPQKVTLY
LRPGQAAAFNVTFRRAKGYPIDLYYLMDLSYSMLDDLRNV
KKLGGDLLRALNEITESGRIGFGSFVDKTVLPFVNTHPDK
LRNPCPNKEKECQPPFAFRHVLKLTNNSNQFQTEVGKQLI
SGNLDAPEGGLDAMMQVAACPEEIGWRKVTRLLVFATDDG
FHFAGDGKLGAILTPNDGRCHLEDNLYKRSNEFDYPSVGQ
LAHKLAENNIQPIFAVTSRMVKTYEKLTEIIPKSAVGELS
EDSSNVVQLIKNAYNKLSSRVFLDHNALPDTLKVTYDSFC
SNGVTHRNQPRGDCDGVQINVPITFQVKVTATECIQEQSF
VIRALGFTDIVTVQVLPQCECRCRDQSRDRSLCHGKGFLE
CGICRCDTGYIGKNC
E:  YNLDVRGARSFSPPRAGRHFGYRVLQVGNGVIVGAPGEGN
STGSLYQCQSGTGHCLPVTLRGSNYTSKYLGMTLATDPTD
GSILACDPGLSRTCDQNTYLSGLCYLFRQNLQGPMLQGRP
GFQECIKGNVDLVFLFDGSMSLQPDEFQKILDFMKDVMKK
LSNTSYQFAAVQFSTSYKTEFDFSDYVKWKDPDALLKHVK
HMLLLTNTFGAINYVATEVFREELGARPDATKVLIIITDG
EATDSGNIDAAKDIIRYIIGIGKHFQTKESQETLHKFASK
PASEFVKILDTFEKLKDLFTELQKKILTSFNMELSSSGIS
ADLSRGHAVVGAVGAKDWAGGFLDLKADLQDDTFIGNEPL
TPEVRAGYLGYTVTWLPSRQKTSLLASGAPRYQHMGRVLL
FQEPQGGGHWSQVQTIHGTQIGSYFGGELCGVDVDQDGET
ELLLIGAPLFYGEQRGGRVFIYQRRQLGFEEVSELQGDPG
YPLGRFGEAITALTDINGDGLVDVAVGAPLEEQGAVYIFN
GRHGGLSPQPSQRIEGTQVLSGIQWFGRSIHGVKDLEGDG
LADVAVGAESQMIVLSSRPV
F:  QECTKFKVSSCRECIESGPGCTWCQKLNFTGPGDPDSIRC
DTRPQLLMRGCAADDIMDPTSLAETQEDQKQLSPQKVTLY
LRPGQAAAFNVTFRRAKGYPIDLYYLMDLSYSMLDDLRNV
KKLGGDLLRALNEITESGRIGFGSFVDKTVLPFVNTHPDK
LRNPCPNKEKECQPPFAFRHVLKLTNNSNQFQTEVGKQLI
SGNLDAPEGGLDAMMQVAACPEEIGWRKVTRLLVFATDDG
FHFAGDGKLGAILTPNDGRCHLEDNLYKRSNEFDYPSVGQ
LAHKLAENNIQPIFAVTSRMVKTYEKLTEIIPKSAVGELS
EDSSNVVQLIKNAYNKLSSRVFLDHNALPDTLKVTYDSFC
SNGVTHRNQPRGDCDGVQINVPITFQVKVTATECIQEQSF
VIRALGFTDIVTVQVLPQCECRCRDQSRDRSLCHGKGFLE
CGICRCDTGYIGKNC
Description (1)  Integrin alpha-L, Integrin beta-2


Functional site
1) chain B
residue 151
type BINDING
sequence D
description in LIMBS binding site => ECO:0000269|PubMed:24385486, ECO:0007744|PDB:4NEH, ECO:0007744|PDB:4NEN
source Swiss-Prot : SWS_FT_FI4
2) chain F
residue 207
type BINDING
sequence N
description in LIMBS binding site => ECO:0000269|PubMed:24385486, ECO:0007744|PDB:4NEH, ECO:0007744|PDB:4NEN
source Swiss-Prot : SWS_FT_FI4
3) chain F
residue 209
type BINDING
sequence D
description in LIMBS binding site => ECO:0000269|PubMed:24385486, ECO:0007744|PDB:4NEH, ECO:0007744|PDB:4NEN
source Swiss-Prot : SWS_FT_FI4
4) chain F
residue 211
type BINDING
sequence P
description in LIMBS binding site => ECO:0000269|PubMed:24385486, ECO:0007744|PDB:4NEH, ECO:0007744|PDB:4NEN
source Swiss-Prot : SWS_FT_FI4
5) chain B
residue 207
type BINDING
sequence N
description in LIMBS binding site => ECO:0000269|PubMed:24385486, ECO:0007744|PDB:4NEH, ECO:0007744|PDB:4NEN
source Swiss-Prot : SWS_FT_FI4
6) chain B
residue 209
type BINDING
sequence D
description in LIMBS binding site => ECO:0000269|PubMed:24385486, ECO:0007744|PDB:4NEH, ECO:0007744|PDB:4NEN
source Swiss-Prot : SWS_FT_FI4
7) chain B
residue 211
type BINDING
sequence P
description in LIMBS binding site => ECO:0000269|PubMed:24385486, ECO:0007744|PDB:4NEH, ECO:0007744|PDB:4NEN
source Swiss-Prot : SWS_FT_FI4
8) chain D
residue 151
type BINDING
sequence D
description in LIMBS binding site => ECO:0000269|PubMed:24385486, ECO:0007744|PDB:4NEH, ECO:0007744|PDB:4NEN
source Swiss-Prot : SWS_FT_FI4
9) chain D
residue 207
type BINDING
sequence N
description in LIMBS binding site => ECO:0000269|PubMed:24385486, ECO:0007744|PDB:4NEH, ECO:0007744|PDB:4NEN
source Swiss-Prot : SWS_FT_FI4
10) chain D
residue 209
type BINDING
sequence D
description in LIMBS binding site => ECO:0000269|PubMed:24385486, ECO:0007744|PDB:4NEH, ECO:0007744|PDB:4NEN
source Swiss-Prot : SWS_FT_FI4
11) chain D
residue 211
type BINDING
sequence P
description in LIMBS binding site => ECO:0000269|PubMed:24385486, ECO:0007744|PDB:4NEH, ECO:0007744|PDB:4NEN
source Swiss-Prot : SWS_FT_FI4
12) chain F
residue 151
type BINDING
sequence D
description in LIMBS binding site => ECO:0000269|PubMed:24385486, ECO:0007744|PDB:4NEH, ECO:0007744|PDB:4NEN
source Swiss-Prot : SWS_FT_FI4
13) chain B
residue 448-459
type prosite
sequence CRCDTGYIGKNC
description EGF_1 EGF-like domain signature 1. CrCdtGyiGKnC
source prosite : PS00022
14) chain B
residue 448-459
type prosite
sequence CRCDTGYIGKNC
description EGF_2 EGF-like domain signature 2. CrCdtGYigkn....C
source prosite : PS01186
15) chain B
residue 114
type BINDING
sequence S
description in MIDAS binding site => ECO:0000269|PubMed:24385486, ECO:0007744|PDB:4NEH, ECO:0007744|PDB:4NEN
source Swiss-Prot : SWS_FT_FI1
16) chain A
residue 569
type BINDING
sequence D
description in MIDAS binding site => ECO:0000269|PubMed:24385486, ECO:0007744|PDB:4NEH, ECO:0007744|PDB:4NEN
source Swiss-Prot : SWS_FT_FI1
17) chain A
residue 573
type BINDING
sequence D
description in MIDAS binding site => ECO:0000269|PubMed:24385486, ECO:0007744|PDB:4NEH, ECO:0007744|PDB:4NEN
source Swiss-Prot : SWS_FT_FI1
18) chain C
residue 443
type BINDING
sequence D
description in MIDAS binding site => ECO:0000269|PubMed:24385486, ECO:0007744|PDB:4NEH, ECO:0007744|PDB:4NEN
source Swiss-Prot : SWS_FT_FI1
19) chain C
residue 445
type BINDING
sequence D
description in MIDAS binding site => ECO:0000269|PubMed:24385486, ECO:0007744|PDB:4NEH, ECO:0007744|PDB:4NEN
source Swiss-Prot : SWS_FT_FI1
20) chain C
residue 447
type BINDING
sequence D
description in MIDAS binding site => ECO:0000269|PubMed:24385486, ECO:0007744|PDB:4NEH, ECO:0007744|PDB:4NEN
source Swiss-Prot : SWS_FT_FI1
21) chain C
residue 451
type BINDING
sequence E
description in MIDAS binding site => ECO:0000269|PubMed:24385486, ECO:0007744|PDB:4NEH, ECO:0007744|PDB:4NEN
source Swiss-Prot : SWS_FT_FI1
22) chain C
residue 505
type BINDING
sequence D
description in MIDAS binding site => ECO:0000269|PubMed:24385486, ECO:0007744|PDB:4NEH, ECO:0007744|PDB:4NEN
source Swiss-Prot : SWS_FT_FI1
23) chain C
residue 507
type BINDING
sequence N
description in MIDAS binding site => ECO:0000269|PubMed:24385486, ECO:0007744|PDB:4NEH, ECO:0007744|PDB:4NEN
source Swiss-Prot : SWS_FT_FI1
24) chain C
residue 509
type BINDING
sequence D
description in MIDAS binding site => ECO:0000269|PubMed:24385486, ECO:0007744|PDB:4NEH, ECO:0007744|PDB:4NEN
source Swiss-Prot : SWS_FT_FI1
25) chain C
residue 513
type BINDING
sequence D
description in MIDAS binding site => ECO:0000269|PubMed:24385486, ECO:0007744|PDB:4NEH, ECO:0007744|PDB:4NEN
source Swiss-Prot : SWS_FT_FI1
26) chain B
residue 116
type BINDING
sequence S
description in MIDAS binding site => ECO:0000269|PubMed:24385486, ECO:0007744|PDB:4NEH, ECO:0007744|PDB:4NEN
source Swiss-Prot : SWS_FT_FI1
27) chain C
residue 565
type BINDING
sequence D
description in MIDAS binding site => ECO:0000269|PubMed:24385486, ECO:0007744|PDB:4NEH, ECO:0007744|PDB:4NEN
source Swiss-Prot : SWS_FT_FI1
28) chain C
residue 569
type BINDING
sequence D
description in MIDAS binding site => ECO:0000269|PubMed:24385486, ECO:0007744|PDB:4NEH, ECO:0007744|PDB:4NEN
source Swiss-Prot : SWS_FT_FI1
29) chain C
residue 573
type BINDING
sequence D
description in MIDAS binding site => ECO:0000269|PubMed:24385486, ECO:0007744|PDB:4NEH, ECO:0007744|PDB:4NEN
source Swiss-Prot : SWS_FT_FI1
30) chain E
residue 443
type BINDING
sequence D
description in MIDAS binding site => ECO:0000269|PubMed:24385486, ECO:0007744|PDB:4NEH, ECO:0007744|PDB:4NEN
source Swiss-Prot : SWS_FT_FI1
31) chain E
residue 445
type BINDING
sequence D
description in MIDAS binding site => ECO:0000269|PubMed:24385486, ECO:0007744|PDB:4NEH, ECO:0007744|PDB:4NEN
source Swiss-Prot : SWS_FT_FI1
32) chain E
residue 447
type BINDING
sequence D
description in MIDAS binding site => ECO:0000269|PubMed:24385486, ECO:0007744|PDB:4NEH, ECO:0007744|PDB:4NEN
source Swiss-Prot : SWS_FT_FI1
33) chain E
residue 451
type BINDING
sequence E
description in MIDAS binding site => ECO:0000269|PubMed:24385486, ECO:0007744|PDB:4NEH, ECO:0007744|PDB:4NEN
source Swiss-Prot : SWS_FT_FI1
34) chain E
residue 505
type BINDING
sequence D
description in MIDAS binding site => ECO:0000269|PubMed:24385486, ECO:0007744|PDB:4NEH, ECO:0007744|PDB:4NEN
source Swiss-Prot : SWS_FT_FI1
35) chain E
residue 507
type BINDING
sequence N
description in MIDAS binding site => ECO:0000269|PubMed:24385486, ECO:0007744|PDB:4NEH, ECO:0007744|PDB:4NEN
source Swiss-Prot : SWS_FT_FI1
36) chain E
residue 509
type BINDING
sequence D
description in MIDAS binding site => ECO:0000269|PubMed:24385486, ECO:0007744|PDB:4NEH, ECO:0007744|PDB:4NEN
source Swiss-Prot : SWS_FT_FI1
37) chain B
residue 212
type BINDING
sequence E
description in MIDAS binding site => ECO:0000269|PubMed:24385486, ECO:0007744|PDB:4NEH, ECO:0007744|PDB:4NEN
source Swiss-Prot : SWS_FT_FI1
38) chain E
residue 513
type BINDING
sequence D
description in MIDAS binding site => ECO:0000269|PubMed:24385486, ECO:0007744|PDB:4NEH, ECO:0007744|PDB:4NEN
source Swiss-Prot : SWS_FT_FI1
39) chain E
residue 565
type BINDING
sequence D
description in MIDAS binding site => ECO:0000269|PubMed:24385486, ECO:0007744|PDB:4NEH, ECO:0007744|PDB:4NEN
source Swiss-Prot : SWS_FT_FI1
40) chain E
residue 569
type BINDING
sequence D
description in MIDAS binding site => ECO:0000269|PubMed:24385486, ECO:0007744|PDB:4NEH, ECO:0007744|PDB:4NEN
source Swiss-Prot : SWS_FT_FI1
41) chain E
residue 573
type BINDING
sequence D
description in MIDAS binding site => ECO:0000269|PubMed:24385486, ECO:0007744|PDB:4NEH, ECO:0007744|PDB:4NEN
source Swiss-Prot : SWS_FT_FI1
42) chain D
residue 114
type BINDING
sequence S
description in MIDAS binding site => ECO:0000269|PubMed:24385486, ECO:0007744|PDB:4NEH, ECO:0007744|PDB:4NEN
source Swiss-Prot : SWS_FT_FI1
43) chain D
residue 116
type BINDING
sequence S
description in MIDAS binding site => ECO:0000269|PubMed:24385486, ECO:0007744|PDB:4NEH, ECO:0007744|PDB:4NEN
source Swiss-Prot : SWS_FT_FI1
44) chain D
residue 212
type BINDING
sequence E
description in MIDAS binding site => ECO:0000269|PubMed:24385486, ECO:0007744|PDB:4NEH, ECO:0007744|PDB:4NEN
source Swiss-Prot : SWS_FT_FI1
45) chain F
residue 114
type BINDING
sequence S
description in MIDAS binding site => ECO:0000269|PubMed:24385486, ECO:0007744|PDB:4NEH, ECO:0007744|PDB:4NEN
source Swiss-Prot : SWS_FT_FI1
46) chain F
residue 116
type BINDING
sequence S
description in MIDAS binding site => ECO:0000269|PubMed:24385486, ECO:0007744|PDB:4NEH, ECO:0007744|PDB:4NEN
source Swiss-Prot : SWS_FT_FI1
47) chain F
residue 212
type BINDING
sequence E
description in MIDAS binding site => ECO:0000269|PubMed:24385486, ECO:0007744|PDB:4NEH, ECO:0007744|PDB:4NEN
source Swiss-Prot : SWS_FT_FI1
48) chain B
residue 1
type MOD_RES
sequence Q
description Pyrrolidone carboxylic acid => ECO:0000305|PubMed:2954816
source Swiss-Prot : SWS_FT_FI7
49) chain D
residue 1
type MOD_RES
sequence Q
description Pyrrolidone carboxylic acid => ECO:0000305|PubMed:2954816
source Swiss-Prot : SWS_FT_FI7
50) chain F
residue 1
type MOD_RES
sequence Q
description Pyrrolidone carboxylic acid => ECO:0000305|PubMed:2954816
source Swiss-Prot : SWS_FT_FI7
51) chain B
residue 28
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:19349973
source Swiss-Prot : SWS_FT_FI8
52) chain D
residue 28
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:19349973
source Swiss-Prot : SWS_FT_FI8
53) chain F
residue 28
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:19349973
source Swiss-Prot : SWS_FT_FI8
54) chain B
residue 94
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19349973, ECO:0000269|PubMed:20033057, ECO:0000269|PubMed:24385486, ECO:0007744|PDB:4NEH, ECO:0007744|PDB:4NEN
source Swiss-Prot : SWS_FT_FI9
55) chain D
residue 94
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19349973, ECO:0000269|PubMed:20033057, ECO:0000269|PubMed:24385486, ECO:0007744|PDB:4NEH, ECO:0007744|PDB:4NEN
source Swiss-Prot : SWS_FT_FI9
56) chain F
residue 94
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19349973, ECO:0000269|PubMed:20033057, ECO:0000269|PubMed:24385486, ECO:0007744|PDB:4NEH, ECO:0007744|PDB:4NEN
source Swiss-Prot : SWS_FT_FI9
57) chain B
residue 190
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:19349973
source Swiss-Prot : SWS_FT_FI10
58) chain D
residue 190
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:19349973
source Swiss-Prot : SWS_FT_FI10
59) chain F
residue 190
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:19349973
source Swiss-Prot : SWS_FT_FI10
60) chain B
residue 232
type CARBOHYD
sequence K
description N-linked (GlcNAc...) asparagine => ECO:0000255
source Swiss-Prot : SWS_FT_FI11
61) chain D
residue 232
type CARBOHYD
sequence K
description N-linked (GlcNAc...) asparagine => ECO:0000255
source Swiss-Prot : SWS_FT_FI11
62) chain F
residue 232
type CARBOHYD
sequence K
description N-linked (GlcNAc...) asparagine => ECO:0000255
source Swiss-Prot : SWS_FT_FI11
63) chain B
residue 119
type BINDING
sequence D
description in ADMIDAS binding site => ECO:0000269|PubMed:20033057, ECO:0007744|PDB:3K6S, ECO:0007744|PDB:3K71, ECO:0007744|PDB:3K72
source Swiss-Prot : SWS_FT_FI2
64) chain E
residue 40
type BINDING
sequence N
description in ADMIDAS binding site => ECO:0000269|PubMed:20033057, ECO:0007744|PDB:3K6S, ECO:0007744|PDB:3K71, ECO:0007744|PDB:3K72
source Swiss-Prot : SWS_FT_FI2
65) chain E
residue 64
type BINDING
sequence N
description in ADMIDAS binding site => ECO:0000269|PubMed:20033057, ECO:0007744|PDB:3K6S, ECO:0007744|PDB:3K71, ECO:0007744|PDB:3K72
source Swiss-Prot : SWS_FT_FI2
66) chain D
residue 119
type BINDING
sequence D
description in ADMIDAS binding site => ECO:0000269|PubMed:20033057, ECO:0007744|PDB:3K6S, ECO:0007744|PDB:3K71, ECO:0007744|PDB:3K72
source Swiss-Prot : SWS_FT_FI2
67) chain F
residue 119
type BINDING
sequence D
description in ADMIDAS binding site => ECO:0000269|PubMed:20033057, ECO:0007744|PDB:3K6S, ECO:0007744|PDB:3K71, ECO:0007744|PDB:3K72
source Swiss-Prot : SWS_FT_FI2
68) chain C
residue 40
type BINDING
sequence N
description in ADMIDAS binding site => ECO:0000269|PubMed:20033057, ECO:0007744|PDB:3K6S, ECO:0007744|PDB:3K71, ECO:0007744|PDB:3K72
source Swiss-Prot : SWS_FT_FI2
69) chain C
residue 64
type BINDING
sequence N
description in ADMIDAS binding site => ECO:0000269|PubMed:20033057, ECO:0007744|PDB:3K6S, ECO:0007744|PDB:3K71, ECO:0007744|PDB:3K72
source Swiss-Prot : SWS_FT_FI2
70) chain B
residue 120
type BINDING
sequence D
description in ADMIDAS binding site => ECO:0000269|PubMed:20033057, ECO:0000269|PubMed:24385486, ECO:0007744|PDB:3K6S, ECO:0007744|PDB:3K71, ECO:0007744|PDB:3K72, ECO:0007744|PDB:4NEH, ECO:0007744|PDB:4NEN
source Swiss-Prot : SWS_FT_FI3
71) chain D
residue 120
type BINDING
sequence D
description in ADMIDAS binding site => ECO:0000269|PubMed:20033057, ECO:0000269|PubMed:24385486, ECO:0007744|PDB:3K6S, ECO:0007744|PDB:3K71, ECO:0007744|PDB:3K72, ECO:0007744|PDB:4NEH, ECO:0007744|PDB:4NEN
source Swiss-Prot : SWS_FT_FI3
72) chain F
residue 120
type BINDING
sequence D
description in ADMIDAS binding site => ECO:0000269|PubMed:20033057, ECO:0000269|PubMed:24385486, ECO:0007744|PDB:3K6S, ECO:0007744|PDB:3K71, ECO:0007744|PDB:3K72, ECO:0007744|PDB:4NEH, ECO:0007744|PDB:4NEN
source Swiss-Prot : SWS_FT_FI3
73) chain B
residue 242
type BINDING
sequence D
description in ADMIDAS binding site and liganded-open conformation => ECO:0000269|PubMed:24385486, ECO:0007744|PDB:4NEN
source Swiss-Prot : SWS_FT_FI5
74) chain D
residue 242
type BINDING
sequence D
description in ADMIDAS binding site and liganded-open conformation => ECO:0000269|PubMed:24385486, ECO:0007744|PDB:4NEN
source Swiss-Prot : SWS_FT_FI5
75) chain F
residue 242
type BINDING
sequence D
description in ADMIDAS binding site and liganded-open conformation => ECO:0000269|PubMed:24385486, ECO:0007744|PDB:4NEN
source Swiss-Prot : SWS_FT_FI5
76) chain B
residue 325
type BINDING
sequence E
description in ADMIDAS binding site and unliganded-closed conformation => ECO:0000269|PubMed:20033057, ECO:0000269|PubMed:24385486, ECO:0007744|PDB:3K6S, ECO:0007744|PDB:3K71, ECO:0007744|PDB:3K72, ECO:0007744|PDB:4NEH
source Swiss-Prot : SWS_FT_FI6
77) chain D
residue 325
type BINDING
sequence E
description in ADMIDAS binding site and unliganded-closed conformation => ECO:0000269|PubMed:20033057, ECO:0000269|PubMed:24385486, ECO:0007744|PDB:3K6S, ECO:0007744|PDB:3K71, ECO:0007744|PDB:3K72, ECO:0007744|PDB:4NEH
source Swiss-Prot : SWS_FT_FI6
78) chain F
residue 325
type BINDING
sequence E
description in ADMIDAS binding site and unliganded-closed conformation => ECO:0000269|PubMed:20033057, ECO:0000269|PubMed:24385486, ECO:0007744|PDB:3K6S, ECO:0007744|PDB:3K71, ECO:0007744|PDB:3K72, ECO:0007744|PDB:4NEH
source Swiss-Prot : SWS_FT_FI6

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