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

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Title Structure basis of RILP recruitment by Rab7
Classification PROTEIN TRANSPORT
Compound Ras-related protein Rab-7
Source Homo sapiens (Human) (RAB7_HUMAN)
Sequence A:  SRKKVLLKVIILGDSGVGKTSLMNQYVNKKFSNQYKATIG
ADFLTKEVMVDDRLVTMQIWDTAGLERFQSLGVAFYRGAD
CCVLVFDVTAPNTFKTLDSWRDEFLIQASPRDPENFPFVV
LGNKIDLENRQVATKRAQAWCYSKNNIPYFETSAKEAINV
EQAFQTIARNALKQETEVELYNE
Description


Functional site

1) chain A
residue 22
type
sequence T
description BINDING SITE FOR RESIDUE MG A 302
source : AC1

2) chain A
residue 40
type
sequence T
description BINDING SITE FOR RESIDUE MG A 302
source : AC1

3) chain A
residue 63
type
sequence D
description BINDING SITE FOR RESIDUE MG A 302
source : AC1

4) chain A
residue 64
type
sequence T
description BINDING SITE FOR RESIDUE MG A 302
source : AC1

5) chain A
residue 17
type
sequence S
description BINDING SITE FOR RESIDUE GTP A 301
source : AC2

6) chain A
residue 18
type
sequence G
description BINDING SITE FOR RESIDUE GTP A 301
source : AC2

7) chain A
residue 19
type
sequence V
description BINDING SITE FOR RESIDUE GTP A 301
source : AC2

8) chain A
residue 20
type
sequence G
description BINDING SITE FOR RESIDUE GTP A 301
source : AC2

9) chain A
residue 21
type
sequence K
description BINDING SITE FOR RESIDUE GTP A 301
source : AC2

10) chain A
residue 22
type
sequence T
description BINDING SITE FOR RESIDUE GTP A 301
source : AC2

11) chain A
residue 23
type
sequence S
description BINDING SITE FOR RESIDUE GTP A 301
source : AC2

12) chain A
residue 33
type
sequence F
description BINDING SITE FOR RESIDUE GTP A 301
source : AC2

13) chain A
residue 34
type
sequence S
description BINDING SITE FOR RESIDUE GTP A 301
source : AC2

14) chain A
residue 35
type
sequence N
description BINDING SITE FOR RESIDUE GTP A 301
source : AC2

15) chain A
residue 37
type
sequence Y
description BINDING SITE FOR RESIDUE GTP A 301
source : AC2

16) chain A
residue 40
type
sequence T
description BINDING SITE FOR RESIDUE GTP A 301
source : AC2

17) chain A
residue 64
type
sequence T
description BINDING SITE FOR RESIDUE GTP A 301
source : AC2

18) chain A
residue 65
type
sequence A
description BINDING SITE FOR RESIDUE GTP A 301
source : AC2

19) chain A
residue 66
type
sequence G
description BINDING SITE FOR RESIDUE GTP A 301
source : AC2

20) chain A
residue 125
type
sequence N
description BINDING SITE FOR RESIDUE GTP A 301
source : AC2

21) chain A
residue 126
type
sequence K
description BINDING SITE FOR RESIDUE GTP A 301
source : AC2

22) chain A
residue 128
type
sequence D
description BINDING SITE FOR RESIDUE GTP A 301
source : AC2

23) chain A
residue 129
type
sequence L
description BINDING SITE FOR RESIDUE GTP A 301
source : AC2

24) chain A
residue 155
type
sequence S
description BINDING SITE FOR RESIDUE GTP A 301
source : AC2

25) chain A
residue 156
type
sequence A
description BINDING SITE FOR RESIDUE GTP A 301
source : AC2

26) chain A
residue 157
type
sequence K
description BINDING SITE FOR RESIDUE GTP A 301
source : AC2

27) chain A
residue 15
type BINDING
sequence G
description BINDING => ECO:0000269|PubMed:15933719, ECO:0000269|PubMed:20028791
source Swiss-Prot : SWS_FT_FI1

28) chain A
residue 34
type BINDING
sequence S
description BINDING => ECO:0000269|PubMed:15933719, ECO:0000269|PubMed:20028791
source Swiss-Prot : SWS_FT_FI1

29) chain A
residue 63
type BINDING
sequence D
description BINDING => ECO:0000269|PubMed:15933719, ECO:0000269|PubMed:20028791
source Swiss-Prot : SWS_FT_FI1

30) chain A
residue 125
type BINDING
sequence N
description BINDING => ECO:0000269|PubMed:15933719, ECO:0000269|PubMed:20028791
source Swiss-Prot : SWS_FT_FI1

31) chain A
residue 156
type BINDING
sequence A
description BINDING => ECO:0000269|PubMed:15933719, ECO:0000269|PubMed:20028791
source Swiss-Prot : SWS_FT_FI1

32) chain A
residue 72
type MOD_RES
sequence S
description Phosphoserine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163
source Swiss-Prot : SWS_FT_FI3

33) chain A
residue 11-24
type prosite
sequence VIILGDSGVGKTSL
description SIGMA54_INTERACT_1 Sigma-54 interaction domain ATP-binding region A signature. VIIlGDSGVGKtsL
source prosite : PS00675


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