eF-site ID 5e6s-F
PDB Code 5e6s
Chain 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 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 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

2) chain F
residue 232
type CARBOHYD
sequence K
description N-linked (GlcNAc...) asparagine => ECO:0000255
source Swiss-Prot : SWS_FT_FI11

3) chain F
residue 1
type MOD_RES
sequence Q
description Pyrrolidone carboxylic acid => ECO:0000305|PubMed:2954816
source Swiss-Prot : SWS_FT_FI7

4) 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

5) 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

6) 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

7) 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

8) 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

9) 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

10) 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

11) 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

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 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

14) 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

15) 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

16) 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


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