eF-site ID 2vc2-ABHL
PDB Code 2vc2
Chain A, B, H, L

click to enlarge
Title Re-refinement of Integrin AlphaIIbBeta3 Headpiece Bound to Antagonist L-739758
Classification CELL ADHESION/IMMUNE SYSTEM
Compound INTEGRIN ALPHA-IIB
Source ORGANISM_COMMON: MOUSE; ORGANISM_SCIENTIFIC: MUS MUSCULUS;
Sequence A:  LNLDPVQLTFYAGPNGSQFGFSLDFHKDSHGRVAIVVGAP
RTLGPSQEETGGVFLCPWRAEGGQCPSLLFDLRDETRNVG
SQTLQTFKARQGLGASVVSWSDVIVACAPWQHWNVLEKTE
EAEKTPVGSCFLAQPESGRRAEYSPCRGNTLSRIYVENDF
SWDKRYCEAGFSSVVTQAGELVLGAPGGYYFLGLLAQAPV
ADIFSSYRPGILLWHVSSQSLSFDSSNPEYFDGYWGYSVA
VGEFDGDLNTTEYVVGAPTWSWTLGAVEILDSYYQRLHRL
RGEQMASYFGHSVAVTDVNGDGRHDLLVGAPLYMESRADR
KLAEVGRVYLFLQPRGPHALGAPSLLLTGTQLYGRFGSAI
APLGDLDRDGYNDIAVAAPYGGPSGRGQVLVFLGQSEGLR
SRPSQVLDSPFPTGSAFGFSLRGAVDIDDNGYPDLIVGAY
GANQVAVYRAQP
B:  GPNICTTRGVSSCQQCLAVSPMCAWCSDEALPLGSPRCDL
KENLLKDNCAPESIEFPVSEARVLEDRPLSDKSSQVTQVS
PQRIALRLRPDDSKNFSIQVRQVEDYPVDIYYLMDLSYSM
KDDLWSIQNLGTKLATQMRKLTSNLRIGFGAFVDKPVSPY
MYISPPEALENPCYDMKTTCLPMFGYKHVLTLTDQVTRFN
EEVKKQSVSRNRDAPEGGFDAIMQATVCDEKIGWRNDASH
LLVFTTDAKTHIALDGRLAGIVQPNDGQCHVGSDNHYSAS
TTMDYPSLGLMTEKLSQKNINLIFAVTENVVNLYQNYSEL
IPGTTVGVLSMDSSNVLQLIVDAYGKIRSKVELEVRDLPE
ELSLSFNATCLNNEVIPGLKSCMGLKIGDTVSFSIEAKVR
GCPQEKEKSFTIKPVGFKDSLIVQVTFDCDCACQAQAEPN
SHRCNNGNGTFECGVCR
H:  EVQLQQSGAELVKPGASVKLSCTASGFNIKDTYVHWVKQR
PEQGLEWIGRIDPANGYTKYDPKFQGKATITADTSSNTAY
LQLSSLTSEDTAVYYCVRPLYDYYAMDYWGQGTSVTVSSA
KTTAPSVYPLAPVCTTGSSVTLGCLVKGYFPEPVTLTWNS
GSLSSGVHTFPAVLQSDLYTLSSSVTVTSSTWPSQSITCN
VAHPASSTKVDKKIEPRGP
L:  DILMTQSPSSMSVSLGDTVSITCHASQGISSNIGWLQQKP
GKSFMGLIYYGTNLVDGVPSRFSGSGSGADYSLTISSLDS
EDFADYYCVQYAQLPYTFGGGTKLEIKRADAAPTVSIFPP
SSEQLTSGGASVVCFLNNFYPKDINVKWKIDGSERQNGVL
NSWTDQDSKDSTYSMSSTLTLTKDEYERHNSYTCEATHKT
STSPIVKSFNRNEC
Description


Functional site

1) chain B
residue 158
type BINDING
sequence D
description in LIMBS binding site => ECO:0000269|PubMed:15378069, ECO:0000269|PubMed:19111664, ECO:0007744|PDB:1TYE, ECO:0007744|PDB:3FCS, ECO:0007744|PDB:3FCU
source Swiss-Prot : SWS_FT_FI4

2) chain B
residue 215
type BINDING
sequence N
description in LIMBS binding site => ECO:0000269|PubMed:15378069, ECO:0000269|PubMed:19111664, ECO:0007744|PDB:1TYE, ECO:0007744|PDB:3FCS, ECO:0007744|PDB:3FCU
source Swiss-Prot : SWS_FT_FI4

3) chain B
residue 217
type BINDING
sequence D
description in LIMBS binding site => ECO:0000269|PubMed:15378069, ECO:0000269|PubMed:19111664, ECO:0007744|PDB:1TYE, ECO:0007744|PDB:3FCS, ECO:0007744|PDB:3FCU
source Swiss-Prot : SWS_FT_FI4

4) chain B
residue 219
type BINDING
sequence P
description in LIMBS binding site => ECO:0000269|PubMed:15378069, ECO:0000269|PubMed:19111664, ECO:0007744|PDB:1TYE, ECO:0007744|PDB:3FCS, ECO:0007744|PDB:3FCU
source Swiss-Prot : SWS_FT_FI4

5) chain B
residue 251
type BINDING
sequence D
description in LIMBS binding site => ECO:0007744|PDB:4G1M
source Swiss-Prot : SWS_FT_FI5

6) chain B
residue 335
type BINDING
sequence M
description in ADMIDAS binding site and unliganded-closed conformation => ECO:0000269|PubMed:11546839, ECO:0000269|PubMed:19111664, ECO:0000269|PubMed:19704023, ECO:0007744|PDB:1JV2, ECO:0007744|PDB:3FCS, ECO:0007744|PDB:3IJE
source Swiss-Prot : SWS_FT_FI6

7) chain B
residue 99
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:15378069, ECO:0000269|PubMed:16263699, ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19111664, ECO:0000269|PubMed:19704023, ECO:0007744|PDB:1TYE, ECO:0007744|PDB:3IJE
source Swiss-Prot : SWS_FT_FI7

8) chain B
residue 320
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:11546839, ECO:0000269|PubMed:15378069, ECO:0000269|PubMed:19111664, ECO:0000269|PubMed:19704023, ECO:0007744|PDB:1JV2, ECO:0007744|PDB:1TYE, ECO:0007744|PDB:3IJE
source Swiss-Prot : SWS_FT_FI8

9) chain B
residue 371
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:11546839, ECO:0000269|PubMed:15378069, ECO:0000269|PubMed:19111664, ECO:0000269|PubMed:19704023, ECO:0007744|PDB:1JV2, ECO:0007744|PDB:1TYE, ECO:0007744|PDB:3IJE
source Swiss-Prot : SWS_FT_FI8

10) chain B
residue 452
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19111664, ECO:0000269|PubMed:19704023, ECO:0007744|PDB:3IJE
source Swiss-Prot : SWS_FT_FI9

11) chain A
residue 247
type BINDING
sequence D
description in MIDAS binding site => ECO:0000269|PubMed:15378069, ECO:0000269|PubMed:19111664, ECO:0007744|PDB:1TYE, ECO:0007744|PDB:3FCS, ECO:0007744|PDB:3FCU
source Swiss-Prot : SWS_FT_FI1

12) chain A
residue 252
type BINDING
sequence E
description in MIDAS binding site => ECO:0000269|PubMed:15378069, ECO:0000269|PubMed:19111664, ECO:0007744|PDB:1TYE, ECO:0007744|PDB:3FCS, ECO:0007744|PDB:3FCU
source Swiss-Prot : SWS_FT_FI1

13) chain A
residue 297
type BINDING
sequence D
description in MIDAS binding site => ECO:0000269|PubMed:15378069, ECO:0000269|PubMed:19111664, ECO:0007744|PDB:1TYE, ECO:0007744|PDB:3FCS, ECO:0007744|PDB:3FCU
source Swiss-Prot : SWS_FT_FI1

14) chain A
residue 299
type BINDING
sequence N
description in MIDAS binding site => ECO:0000269|PubMed:15378069, ECO:0000269|PubMed:19111664, ECO:0007744|PDB:1TYE, ECO:0007744|PDB:3FCS, ECO:0007744|PDB:3FCU
source Swiss-Prot : SWS_FT_FI1

15) chain A
residue 301
type BINDING
sequence D
description in MIDAS binding site => ECO:0000269|PubMed:15378069, ECO:0000269|PubMed:19111664, ECO:0007744|PDB:1TYE, ECO:0007744|PDB:3FCS, ECO:0007744|PDB:3FCU
source Swiss-Prot : SWS_FT_FI1

16) chain A
residue 250
type BINDING
sequence T
description in MIDAS binding site => ECO:0000269|PubMed:15378069, ECO:0000269|PubMed:19111664, ECO:0007744|PDB:1TYE, ECO:0007744|PDB:3FCS, ECO:0007744|PDB:3FCU
source Swiss-Prot : SWS_FT_FI1

17) chain A
residue 434
type BINDING
sequence D
description in MIDAS binding site => ECO:0000269|PubMed:15378069, ECO:0000269|PubMed:19111664, ECO:0007744|PDB:1TYE, ECO:0007744|PDB:3FCS, ECO:0007744|PDB:3FCU
source Swiss-Prot : SWS_FT_FI1

18) chain B
residue 121
type BINDING
sequence S
description in MIDAS binding site => ECO:0000269|PubMed:15378069, ECO:0000269|PubMed:19111664, ECO:0007744|PDB:1TYE, ECO:0007744|PDB:3FCS, ECO:0007744|PDB:3FCU
source Swiss-Prot : SWS_FT_FI1

19) chain B
residue 220
type BINDING
sequence E
description in MIDAS binding site => ECO:0000269|PubMed:15378069, ECO:0000269|PubMed:19111664, ECO:0007744|PDB:1TYE, ECO:0007744|PDB:3FCS, ECO:0007744|PDB:3FCU
source Swiss-Prot : SWS_FT_FI1

20) chain A
residue 303
type BINDING
sequence R
description in MIDAS binding site => ECO:0000269|PubMed:15378069, ECO:0000269|PubMed:19111664, ECO:0007744|PDB:1TYE, ECO:0007744|PDB:3FCS, ECO:0007744|PDB:3FCU
source Swiss-Prot : SWS_FT_FI1

21) chain A
residue 305
type BINDING
sequence D
description in MIDAS binding site => ECO:0000269|PubMed:15378069, ECO:0000269|PubMed:19111664, ECO:0007744|PDB:1TYE, ECO:0007744|PDB:3FCS, ECO:0007744|PDB:3FCU
source Swiss-Prot : SWS_FT_FI1

22) chain A
residue 365
type BINDING
sequence D
description in MIDAS binding site => ECO:0000269|PubMed:15378069, ECO:0000269|PubMed:19111664, ECO:0007744|PDB:1TYE, ECO:0007744|PDB:3FCS, ECO:0007744|PDB:3FCU
source Swiss-Prot : SWS_FT_FI1

23) chain A
residue 367
type BINDING
sequence D
description in MIDAS binding site => ECO:0000269|PubMed:15378069, ECO:0000269|PubMed:19111664, ECO:0007744|PDB:1TYE, ECO:0007744|PDB:3FCS, ECO:0007744|PDB:3FCU
source Swiss-Prot : SWS_FT_FI1

24) chain A
residue 369
type BINDING
sequence D
description in MIDAS binding site => ECO:0000269|PubMed:15378069, ECO:0000269|PubMed:19111664, ECO:0007744|PDB:1TYE, ECO:0007744|PDB:3FCS, ECO:0007744|PDB:3FCU
source Swiss-Prot : SWS_FT_FI1

25) chain A
residue 371
type BINDING
sequence Y
description in MIDAS binding site => ECO:0000269|PubMed:15378069, ECO:0000269|PubMed:19111664, ECO:0007744|PDB:1TYE, ECO:0007744|PDB:3FCS, ECO:0007744|PDB:3FCU
source Swiss-Prot : SWS_FT_FI1

26) chain A
residue 373
type BINDING
sequence D
description in MIDAS binding site => ECO:0000269|PubMed:15378069, ECO:0000269|PubMed:19111664, ECO:0007744|PDB:1TYE, ECO:0007744|PDB:3FCS, ECO:0007744|PDB:3FCU
source Swiss-Prot : SWS_FT_FI1

27) chain A
residue 426
type BINDING
sequence D
description in MIDAS binding site => ECO:0000269|PubMed:15378069, ECO:0000269|PubMed:19111664, ECO:0007744|PDB:1TYE, ECO:0007744|PDB:3FCS, ECO:0007744|PDB:3FCU
source Swiss-Prot : SWS_FT_FI1

28) chain A
residue 428
type BINDING
sequence D
description in MIDAS binding site => ECO:0000269|PubMed:15378069, ECO:0000269|PubMed:19111664, ECO:0007744|PDB:1TYE, ECO:0007744|PDB:3FCS, ECO:0007744|PDB:3FCU
source Swiss-Prot : SWS_FT_FI1

29) chain A
residue 430
type BINDING
sequence N
description in MIDAS binding site => ECO:0000269|PubMed:15378069, ECO:0000269|PubMed:19111664, ECO:0007744|PDB:1TYE, ECO:0007744|PDB:3FCS, ECO:0007744|PDB:3FCU
source Swiss-Prot : SWS_FT_FI1

30) chain A
residue 432
type BINDING
sequence Y
description in MIDAS binding site => ECO:0000269|PubMed:15378069, ECO:0000269|PubMed:19111664, ECO:0007744|PDB:1TYE, ECO:0007744|PDB:3FCS, ECO:0007744|PDB:3FCU
source Swiss-Prot : SWS_FT_FI1

31) chain B
residue 123
type BINDING
sequence S
description in MIDAS binding site => ECO:0000269|PubMed:15378069, ECO:0000269|PubMed:19111664, ECO:0007744|PDB:1TYE, ECO:0007744|PDB:3FCU
source Swiss-Prot : SWS_FT_FI2

32) chain B
residue 127
type BINDING
sequence D
description in ADMIDAS binding site => ECO:0000269|PubMed:11546839, ECO:0000269|PubMed:15378069, ECO:0000269|PubMed:19111664, ECO:0000269|PubMed:19704023, ECO:0007744|PDB:1JV2, ECO:0007744|PDB:1TYE, ECO:0007744|PDB:3FCS, ECO:0007744|PDB:3FCU, ECO:0007744|PDB:3IJE
source Swiss-Prot : SWS_FT_FI3

33) chain B
residue 126
type BINDING
sequence D
description in ADMIDAS binding site => ECO:0000269|PubMed:11546839, ECO:0000269|PubMed:15378069, ECO:0000269|PubMed:19111664, ECO:0000269|PubMed:19704023, ECO:0007744|PDB:1JV2, ECO:0007744|PDB:1TYE, ECO:0007744|PDB:3FCS, ECO:0007744|PDB:3FCU, ECO:0007744|PDB:3IJE
source Swiss-Prot : SWS_FT_FI3

34) chain L
residue 192-198
type prosite
sequence YTCEATH
description IG_MHC Immunoglobulins and major histocompatibility complex proteins signature. YTCEATH
source prosite : PS00290


Display surface

Download
Links