eF-site ID 1avr-A
PDB Code 1avr
Chain A

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Title CRYSTAL AND MOLECULAR STRUCTURE OF HUMAN ANNEXIN V AFTER REFINEMENT. IMPLICATIONS FOR STRUCTURE, MEMBRANE BINDING AND ION CHANNEL FORMATION OF THE ANNEXIN FAMILY OF PROTEINS
Classification CALCIUM/PHOSPHOLIPID BINDING
Compound ANNEXIN V
Source (ANXA5_HUMAN)
Sequence A:  QVLRGTVTDFPGFDERADAETLRKAMKGLGTDEESILTLL
TSRSNAQRQEISAAFKTLFGRDLLDDLKSELTGKFEKLIV
ALMKPSRLYDAYELKHALKGAGTNEKVLTEIIASRTPEEL
RAIKQVYEEEYGSSLEDDVVGDTSGYYQRMLVVLLQANRD
PDAGIDEAQVEQDAQALFQAGELKWGTDEEKFITIFGTRS
VSHLRKVFDKYMTISGFQIEETIDRETSGNLEQLLLAVVK
SIRSIPAYLAETLYYAMKGAGTDDHTLIRVMVSRSEIDLF
NIRKEFRKNFATSLYSMIKGDTSGDYKKALLLLCGED
Description


Functional site

1) chain A
residue 100
type
sequence L
description BINDING SITE FOR RESIDUE CA A 321
source : AC1

2) chain A
residue 102
type
sequence G
description BINDING SITE FOR RESIDUE CA A 321
source : AC1

3) chain A
residue 104
type
sequence G
description BINDING SITE FOR RESIDUE CA A 321
source : AC1

4) chain A
residue 144
type
sequence D
description BINDING SITE FOR RESIDUE CA A 321
source : AC1

5) chain A
residue 259
type
sequence M
description BINDING SITE FOR RESIDUE CA A 322
source : AC2

6) chain A
residue 261
type
sequence G
description BINDING SITE FOR RESIDUE CA A 322
source : AC2

7) chain A
residue 263
type
sequence G
description BINDING SITE FOR RESIDUE CA A 322
source : AC2

8) chain A
residue 303
type
sequence D
description BINDING SITE FOR RESIDUE CA A 322
source : AC2

9) chain A
residue 28
type
sequence M
description BINDING SITE FOR RESIDUE CA A 323
source : AC3

10) chain A
residue 30
type
sequence G
description BINDING SITE FOR RESIDUE CA A 323
source : AC3

11) chain A
residue 32
type
sequence G
description BINDING SITE FOR RESIDUE CA A 323
source : AC3

12) chain A
residue 72
type
sequence E
description BINDING SITE FOR RESIDUE CA A 323
source : AC3

13) chain A
residue 33
type
sequence T
description BINDING SITE FOR RESIDUE CA A 324
source : AC4

14) chain A
residue 35
type
sequence E
description BINDING SITE FOR RESIDUE CA A 324
source : AC4

15) chain A
residue 70
type
sequence K
description BINDING SITE FOR RESIDUE CA A 325
source : AC5

16) chain A
residue 73
type
sequence L
description BINDING SITE FOR RESIDUE CA A 325
source : AC5

17) chain A
residue 78
type
sequence E
description BINDING SITE FOR RESIDUE CA A 325
source : AC5

18) chain A
residue 25
type
sequence R
description BINDING SITE FOR RESIDUE SO4 A 550
source : AC6

19) chain A
residue 30
type
sequence G
description BINDING SITE FOR RESIDUE SO4 A 550
source : AC6

20) chain A
residue 63
type
sequence R
description BINDING SITE FOR RESIDUE SO4 A 550
source : AC6

21) chain A
residue 285
type
sequence R
description BINDING SITE FOR RESIDUE SO4 A 551
source : AC7

22) chain A
residue 286
type
sequence K
description BINDING SITE FOR RESIDUE SO4 A 551
source : AC7

23) chain A
residue 32-84
type prosite
sequence GTDEESILTLLTSRSNAQRQEISAAFKTLFGRDLLDDLKS
ELTGKFEKLIVAL
description ANNEXIN_1 Annexin repeat signature. GTdeesiltlLtsRsnaQrqEisaaFktlfgrdLlddLkseltGkfeklIvaL
source prosite : PS00223

24) chain A
residue 104-156
type prosite
sequence GTNEKVLTEIIASRTPEELRAIKQVYEEEYGSSLEDDVVG
DTSGYYQRMLVVL
description ANNEXIN_1 Annexin repeat signature. GTdeesiltlLtsRsnaQrqEisaaFktlfgrdLlddLkseltGkfeklIvaL
source prosite : PS00223

25) chain A
residue 188-240
type prosite
sequence GTDEEKFITIFGTRSVSHLRKVFDKYMTISGFQIEETIDR
ETSGNLEQLLLAV
description ANNEXIN_1 Annexin repeat signature. GTdeesiltlLtsRsnaQrqEisaaFktlfgrdLlddLkseltGkfeklIvaL
source prosite : PS00223

26) chain A
residue 263-315
type prosite
sequence GTDDHTLIRVMVSRSEIDLFNIRKEFRKNFATSLYSMIKG
DTSGDYKKALLLL
description ANNEXIN_1 Annexin repeat signature. GTdeesiltlLtsRsnaQrqEisaaFktlfgrdLlddLkseltGkfeklIvaL
source prosite : PS00223

27) chain A
residue 30
type CROSSLNK
sequence G
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate => ECO:0007744|PubMed:25772364, ECO:0007744|PubMed:28112733
source Swiss-Prot : SWS_FT_FI6

28) chain A
residue 3
type MOD_RES
sequence Q
description N-acetylalanine => ECO:0007744|PubMed:19413330
source Swiss-Prot : SWS_FT_FI1

29) chain A
residue 38
type MOD_RES
sequence I
description Phosphoserine => ECO:0000250|UniProtKB:P48036
source Swiss-Prot : SWS_FT_FI2

30) chain A
residue 71
type MOD_RES
sequence S
description N6-acetyllysine => ECO:0007744|PubMed:19608861
source Swiss-Prot : SWS_FT_FI3

31) chain A
residue 77
type MOD_RES
sequence F
description N6-acetyllysine => ECO:0007744|PubMed:19608861
source Swiss-Prot : SWS_FT_FI3

32) chain A
residue 80
type MOD_RES
sequence L
description N6-acetyllysine => ECO:0007744|PubMed:19608861
source Swiss-Prot : SWS_FT_FI3

33) chain A
residue 98
type MOD_RES
sequence H
description N6-acetyllysine => ECO:0007744|PubMed:19608861
source Swiss-Prot : SWS_FT_FI3

34) chain A
residue 102
type MOD_RES
sequence G
description N6-acetyllysine => ECO:0007744|PubMed:16916647
source Swiss-Prot : SWS_FT_FI4

35) chain A
residue 291
type MOD_RES
sequence N
description N6-succinyllysine => ECO:0000250|UniProtKB:P48036
source Swiss-Prot : SWS_FT_FI5


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