eF-site ID 3v4p-ABCDHLMN
PDB Code 3v4p
Chain A, B, C, D, H, L, M, N

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Title crystal structure of a4b7 headpiece complexed with Fab ACT-1
Classification CELL ADHESION
Compound Integrin alpha-4
Source (3V4P)
Sequence A:  YNVDTESALLYQGPHNTLFGYSVVLHSHGANRWLLVGAPT
ANWLANASVINPGAIYRCRIGKNPGQTCEQLQLGSPNGEP
CGKTCLEERDNQWLGVTLSRQPGENGSIVTCGHRWKNIFY
IKNENKLPTGGCYGVPPDLRTELSKRIAPCYQDYVKKFGE
NFASCQAGISSFYTKDLIVMGAPGSSYWTGSLFVYNITTN
KYKAFLDKQNQVKFGSYLGYSVGAGHFRSQHTTEVVGGAP
QHEQIGKAYIFSIDEKELNILHEMKGKKLGSYFGASVCAV
DLNADGFSDLLVGAPMQSTIREEGRVFVYINSGSGAVMNA
METNLVGSDKYAARFGESIVNLGDIDNDGFEDVAIGAPQE
DDLQGAIYIYNGRADGISSTFSQRIEGLQISKSLSMFGQS
ISGQIDADNNGYVDVAVGAFRSDSAVLLRTRPVVIVDASL
SHPESVNRTKFDCVENGWPSVCIDLTLCFSYKGKEVPGYI
VLFYNMSLDVNRKAESPPRFYFSSNGTSDVITGSIQVSSR
EANCRTHQAFMRKDVRDILTPIQIEAAYHLGPHSTEEFPP
LQPILQQKKEKDIMKKTINFAR
B:  RGQQEVLQDQPLSQGARGEGATQLAPQRVRVTLRPGEPQQ
LQVRFLRAEGYPVDLYYLMDLSYSMKDDLERVRQLGHALL
VRLQEVTHSVRIGFGSFVDKTVLPFVSTVPSKLRHPCPTR
LERCQSPFSFHHVLSLTGDAQAFEREVGRQSVSGNLDSPE
GGFDAILQAALCQEQIGWRNVSRLLVFTSDDTFHTAGDGK
LGGIFMPSDGHCHLDSNGLYSRSTEFDYPSVGQVAQALSA
ANIQPIFAVTSAALPVYQELSKLIPKSAVGELSEDSSNVV
QLIMDAYNSLSSTVTLEHSSLPPGVHISYESQCEGPEKRE
GKAEDRGQCNHVRINQTVTFWVSLQATHCLPEPHLLRLRA
LGFSEELIVELHTLC
C:  YNVDTESALLYQGPHNTLFGYSVVLHSHGANRWLLVGAPT
ANWLANASVINPGAIYRCRIGKNPGQTCEQLQLGSPNGEP
CGKTCLEERDNQWLGVTLSRQPGENGSIVTCGHRWKNIFY
IKNENKLPTGGCYGVPPDLRTELSKRIAPCYQDYVKKFGE
NFASCQAGISSFYTKDLIVMGAPGSSYWTGSLFVYNITTN
KYKAFLDKQNQVKFGSYLGYSVGAGHFRSQHTTEVVGGAP
QHEQIGKAYIFSIDEKELNILHEMKGKKLGSYFGASVCAV
DLNADGFSDLLVGAPMQSTIREEGRVFVYINSGSGAVMNA
METNLVGSDKYAARFGESIVNLGDIDNDGFEDVAIGAPQE
DDLQGAIYIYNGRADGISSTFSQRIEGLQISKSLSMFGQS
ISGQIDADNNGYVDVAVGAFRSDSAVLLRTRPVVIVDASL
SHPESVNRTKFDCVENGWPSVCIDLTLCFSYKGKEVPGYI
VLFYNMSLDVNRKAESPPRFYFSSNGTSDVITGSIQVSSR
EANCRTHQAFMRKDVRDILTPIQIEAAYHLGPHTEEFPPL
QPILQQKKEKDIMKKTINFAR
D:  RGQQEVLQDQPLSQGARGEGATQLAPQRVRVTLRPGEPQQ
LQVRFLRAEGYPVDLYYLMDLSYSMKDDLERVRQLGHALL
VRLQEVTHSVRIGFGSFVDKTVLPFVSTVPSKLRHPCPTR
LERCQSPFSFHHVLSLTGDAQAFEREVGRQSVSGNLDSPE
GGFDAILQAALCQEQIGWRNVSRLLVFTSDDTFHTAGDGK
LGGIFMPSDGHCHLDSNGLYSRSTEFDYPSVGQVAQALSA
ANIQPIFAVTSAALPVYQELSKLIPKSAVGELSEDSSNVV
QLIMDAYNSLSSTVTLEHSSLPPGVHISYESQCEGPEKRE
GKAEDRGQCNHVRINQTVTFWVSLQATHCLPEPHLLRLRA
LGFSEELIVELHTLC
H:  QVQLQQPGAELVKPGTSVKLSCKGYGYTFTSYWMHWVKQR
PGQGLEWIGEIDPSESNTNYNQKFKGKATLTVDISSSTAY
MQLSSLTSEDSAVYYCARGGYDGWDYAIDYWGQGTSVTVS
SAKTTPPSVYPLAPSMVTLGCLVKGYFPEPVTVTWNSGSL
SSGVHTFPAVLESDLYTLSSSVTVPSSPRPSETVTCNVAH
PASSTKVDKKI
L:  DVVVTQTPLSLPVSFGDQVSISCRSSQSLAKSYGNTYLSW
YLHKPGQSPQLLIYGISNRFSGVPDRFSGSGSGTDFTLKI
STIKPEDLGMYYCLQGTHQPYTFGGGTKLEIKRADAAPTV
SIFPPSSEQLTSGGASVVCFLNNFYPKDINVKWNIDGSER
QNGVLNSWTDQDSKDSTYSMSSTLTLTKDEYERHNSYTCE
ATHKTSTSPIVKSFNRN
M:  QVQLQQPGAELVKPGTSVKLSCKGYGYTFTSYWMHWVKQR
PGQGLEWIGEIDPSESNTNYNQKFKGKATLTVDISSSTAY
MQLSSLTSEDSAVYYCARGGYDGWDYAIDYWGQGTSVTVS
SAKTTPPSVYPLAPSMVTLGCLVKGYFPEPVTVTWNSGSL
SSGVHTFPAVLESDLYTLSSSVTVPSSPRPSETVTCNVAH
PASSTKVDKKI
N:  DVVVTQTPLSLPVSFGDQVSISCRSSQSLAKSYGNTYLSW
YLHKPGQSPQLLIYGISNRFSGVPDRFSGSGSGTDFTLKI
STIKPEDLGMYYCLQGTHQPYTFGGGTKLEIKRADAAPTV
SIFPPSSEQLTSGGASVVCFLNNFYPKDINVKWNIDGSER
QNGVLNSWTDQDSKDSTYSMSSTLTLTKDEYERHNSYTCE
ATHKTSTSPIVKSFNRN
Description (1)  Integrin alpha-4, Integrin beta-7, heavy chain, light chain


Functional site
1) chain L
residue 197-203
type prosite
sequence YTCEATH
description IG_MHC Immunoglobulins and major histocompatibility complex proteins signature. YTCEATH
source prosite : PS00290
2) chain B
residue 142
type BINDING
sequence S
description in MIDAS binding site => ECO:0000269|PubMed:22232704, ECO:0007744|PDB:3V4V
source Swiss-Prot : SWS_FT_FI1
3) chain A
residue 408
type BINDING
sequence D
description in MIDAS binding site => ECO:0000269|PubMed:22232704, ECO:0007744|PDB:3V4V
source Swiss-Prot : SWS_FT_FI1
4) chain A
residue 410
type BINDING
sequence N
description in MIDAS binding site => ECO:0000269|PubMed:22232704, ECO:0007744|PDB:3V4V
source Swiss-Prot : SWS_FT_FI1
5) chain A
residue 412
type BINDING
sequence Y
description in MIDAS binding site => ECO:0000269|PubMed:22232704, ECO:0007744|PDB:3V4V
source Swiss-Prot : SWS_FT_FI1
6) chain A
residue 414
type BINDING
sequence D
description in MIDAS binding site => ECO:0000269|PubMed:22232704, ECO:0007744|PDB:3V4V
source Swiss-Prot : SWS_FT_FI1
7) chain C
residue 281
type BINDING
sequence D
description in MIDAS binding site => ECO:0000269|PubMed:22232704, ECO:0007744|PDB:3V4V
source Swiss-Prot : SWS_FT_FI1
8) chain C
residue 283
type BINDING
sequence N
description in MIDAS binding site => ECO:0000269|PubMed:22232704, ECO:0007744|PDB:3V4V
source Swiss-Prot : SWS_FT_FI1
9) chain C
residue 285
type BINDING
sequence D
description in MIDAS binding site => ECO:0000269|PubMed:22232704, ECO:0007744|PDB:3V4V
source Swiss-Prot : SWS_FT_FI1
10) chain C
residue 289
type BINDING
sequence D
description in MIDAS binding site => ECO:0000269|PubMed:22232704, ECO:0007744|PDB:3V4V
source Swiss-Prot : SWS_FT_FI1
11) chain C
residue 344
type BINDING
sequence D
description in MIDAS binding site => ECO:0000269|PubMed:22232704, ECO:0007744|PDB:3V4V
source Swiss-Prot : SWS_FT_FI1
12) chain C
residue 346
type BINDING
sequence D
description in MIDAS binding site => ECO:0000269|PubMed:22232704, ECO:0007744|PDB:3V4V
source Swiss-Prot : SWS_FT_FI1
13) chain B
residue 144
type BINDING
sequence S
description in MIDAS binding site => ECO:0000269|PubMed:22232704, ECO:0007744|PDB:3V4V
source Swiss-Prot : SWS_FT_FI1
14) chain C
residue 348
type BINDING
sequence D
description in MIDAS binding site => ECO:0000269|PubMed:22232704, ECO:0007744|PDB:3V4V
source Swiss-Prot : SWS_FT_FI1
15) chain C
residue 352
type BINDING
sequence D
description in MIDAS binding site => ECO:0000269|PubMed:22232704, ECO:0007744|PDB:3V4V
source Swiss-Prot : SWS_FT_FI1
16) chain C
residue 406
type BINDING
sequence D
description in MIDAS binding site => ECO:0000269|PubMed:22232704, ECO:0007744|PDB:3V4V
source Swiss-Prot : SWS_FT_FI1
17) chain C
residue 408
type BINDING
sequence D
description in MIDAS binding site => ECO:0000269|PubMed:22232704, ECO:0007744|PDB:3V4V
source Swiss-Prot : SWS_FT_FI1
18) chain C
residue 410
type BINDING
sequence N
description in MIDAS binding site => ECO:0000269|PubMed:22232704, ECO:0007744|PDB:3V4V
source Swiss-Prot : SWS_FT_FI1
19) chain C
residue 412
type BINDING
sequence Y
description in MIDAS binding site => ECO:0000269|PubMed:22232704, ECO:0007744|PDB:3V4V
source Swiss-Prot : SWS_FT_FI1
20) chain C
residue 414
type BINDING
sequence D
description in MIDAS binding site => ECO:0000269|PubMed:22232704, ECO:0007744|PDB:3V4V
source Swiss-Prot : SWS_FT_FI1
21) chain D
residue 142
type BINDING
sequence S
description in MIDAS binding site => ECO:0000269|PubMed:22232704, ECO:0007744|PDB:3V4V
source Swiss-Prot : SWS_FT_FI1
22) chain D
residue 144
type BINDING
sequence S
description in MIDAS binding site => ECO:0000269|PubMed:22232704, ECO:0007744|PDB:3V4V
source Swiss-Prot : SWS_FT_FI1
23) chain A
residue 344
type BINDING
sequence D
description in MIDAS binding site => ECO:0000269|PubMed:22232704, ECO:0007744|PDB:3V4V
source Swiss-Prot : SWS_FT_FI1
24) chain A
residue 346
type BINDING
sequence D
description in MIDAS binding site => ECO:0000269|PubMed:22232704, ECO:0007744|PDB:3V4V
source Swiss-Prot : SWS_FT_FI1
25) chain A
residue 348
type BINDING
sequence D
description in MIDAS binding site => ECO:0000269|PubMed:22232704, ECO:0007744|PDB:3V4V
source Swiss-Prot : SWS_FT_FI1
26) chain A
residue 352
type BINDING
sequence D
description in MIDAS binding site => ECO:0000269|PubMed:22232704, ECO:0007744|PDB:3V4V
source Swiss-Prot : SWS_FT_FI1
27) chain A
residue 406
type BINDING
sequence D
description in MIDAS binding site => ECO:0000269|PubMed:22232704, ECO:0007744|PDB:3V4V
source Swiss-Prot : SWS_FT_FI1
28) chain B
residue 415
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:22232704, ECO:0007744|PDB:3V4V
source Swiss-Prot : SWS_FT_FI10
29) chain D
residue 415
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:22232704, ECO:0007744|PDB:3V4V
source Swiss-Prot : SWS_FT_FI10
30) chain B
residue 147
type BINDING
sequence D
description in ADMIDAS binding site => ECO:0000269|PubMed:22232704, ECO:0007744|PDB:3V4V
source Swiss-Prot : SWS_FT_FI2
31) chain D
residue 147
type BINDING
sequence D
description in ADMIDAS binding site => ECO:0000269|PubMed:22232704, ECO:0007744|PDB:3V4V
source Swiss-Prot : SWS_FT_FI2
32) chain B
residue 148
type BINDING
sequence D
description in ADMIDAS binding site => ECO:0000269|PubMed:22232704, ECO:0007744|PDB:3V4P
source Swiss-Prot : SWS_FT_FI3
33) chain D
residue 148
type BINDING
sequence D
description in ADMIDAS binding site => ECO:0000269|PubMed:22232704, ECO:0007744|PDB:3V4P
source Swiss-Prot : SWS_FT_FI3
34) chain A
residue 196
type BINDING
sequence N
description in ADMIDAS binding site => ECO:0000269|PubMed:22232704, ECO:0007744|PDB:3V4P
source Swiss-Prot : SWS_FT_FI3
35) chain C
residue 46
type BINDING
sequence N
description in ADMIDAS binding site => ECO:0000269|PubMed:22232704, ECO:0007744|PDB:3V4P
source Swiss-Prot : SWS_FT_FI3
36) chain C
residue 105
type BINDING
sequence N
description in ADMIDAS binding site => ECO:0000269|PubMed:22232704, ECO:0007744|PDB:3V4P
source Swiss-Prot : SWS_FT_FI3
37) chain C
residue 196
type BINDING
sequence N
description in ADMIDAS binding site => ECO:0000269|PubMed:22232704, ECO:0007744|PDB:3V4P
source Swiss-Prot : SWS_FT_FI3
38) chain B
residue 179
type BINDING
sequence D
description in LIMBS binding site => ECO:0000269|PubMed:22232704, ECO:0007744|PDB:3V4P, ECO:0007744|PDB:3V4V
source Swiss-Prot : SWS_FT_FI4
39) chain B
residue 235
type BINDING
sequence N
description in LIMBS binding site => ECO:0000269|PubMed:22232704, ECO:0007744|PDB:3V4P, ECO:0007744|PDB:3V4V
source Swiss-Prot : SWS_FT_FI4
40) chain B
residue 237
type BINDING
sequence D
description in LIMBS binding site => ECO:0000269|PubMed:22232704, ECO:0007744|PDB:3V4P, ECO:0007744|PDB:3V4V
source Swiss-Prot : SWS_FT_FI4
41) chain B
residue 239
type BINDING
sequence P
description in LIMBS binding site => ECO:0000269|PubMed:22232704, ECO:0007744|PDB:3V4P, ECO:0007744|PDB:3V4V
source Swiss-Prot : SWS_FT_FI4
42) chain D
residue 179
type BINDING
sequence D
description in LIMBS binding site => ECO:0000269|PubMed:22232704, ECO:0007744|PDB:3V4P, ECO:0007744|PDB:3V4V
source Swiss-Prot : SWS_FT_FI4
43) chain D
residue 235
type BINDING
sequence N
description in LIMBS binding site => ECO:0000269|PubMed:22232704, ECO:0007744|PDB:3V4P, ECO:0007744|PDB:3V4V
source Swiss-Prot : SWS_FT_FI4
44) chain D
residue 237
type BINDING
sequence D
description in LIMBS binding site => ECO:0000269|PubMed:22232704, ECO:0007744|PDB:3V4P, ECO:0007744|PDB:3V4V
source Swiss-Prot : SWS_FT_FI4
45) chain D
residue 239
type BINDING
sequence P
description in LIMBS binding site => ECO:0000269|PubMed:22232704, ECO:0007744|PDB:3V4P, ECO:0007744|PDB:3V4V
source Swiss-Prot : SWS_FT_FI4
46) chain B
residue 240
type BINDING
sequence E
description in MIDAS binding site => ECO:0000269|PubMed:22232704, ECO:0007744|PDB:3V4P, ECO:0007744|PDB:3V4V
source Swiss-Prot : SWS_FT_FI5
47) chain D
residue 240
type BINDING
sequence E
description in MIDAS binding site => ECO:0000269|PubMed:22232704, ECO:0007744|PDB:3V4P, ECO:0007744|PDB:3V4V
source Swiss-Prot : SWS_FT_FI5
48) chain B
residue 270
type BINDING
sequence D
description in ADMIDAS binding site and liganded-open conformation => ECO:0000250|UniProtKB:P05107
source Swiss-Prot : SWS_FT_FI6
49) chain D
residue 270
type BINDING
sequence D
description in ADMIDAS binding site and liganded-open conformation => ECO:0000250|UniProtKB:P05107
source Swiss-Prot : SWS_FT_FI6
50) chain B
residue 354
type BINDING
sequence E
description in ADMIDAS binding site and unliganded-closed conformation => ECO:0000269|PubMed:22232704, ECO:0007744|PDB:3V4P, ECO:0007744|PDB:3V4V
source Swiss-Prot : SWS_FT_FI7
51) chain D
residue 354
type BINDING
sequence E
description in ADMIDAS binding site and unliganded-closed conformation => ECO:0000269|PubMed:22232704, ECO:0007744|PDB:3V4P, ECO:0007744|PDB:3V4V
source Swiss-Prot : SWS_FT_FI7
52) chain B
residue 260
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:22232704, ECO:0007744|PDB:3V4P, ECO:0007744|PDB:3V4V
source Swiss-Prot : SWS_FT_FI9
53) chain D
residue 260
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:22232704, ECO:0007744|PDB:3V4P, ECO:0007744|PDB:3V4V
source Swiss-Prot : SWS_FT_FI9

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