eF-site ID 6u3x-B
PDB Code 6u3x
Chain B

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Title PCSK9 in complex with compound 2
Classification HYDROLASE
Compound Proprotein convertase subtilisin/kexin type 9
Source (PCSK9_HUMAN)
Sequence B:  SIPWNLERITPPRYRGGSLVEVYLLDTSIQSDHREIEGRV
MVTDFENVPEEDASKCDSHGTHLAGVVSGRDAGVAKGASM
RSLRVLNCQGKGTVSGTLIGLEFIRKSQLVQPVGPLVVLL
PLAGGYSRVLNAACQRLARAGVVLVTAAGNFRDDACLYSP
ASAPEVITVGATNAQDQPVTLGTLGTNFGRCVDLFAPGED
IIGASSDCSTCFVSQSGTSQAAAHVAGIAAMMLSAEPELT
LAELRQRLIHFSAKDVINEAWFPEDQRVLTPNLVAALPPS
THGWQLFCRTVWSAHSGPTRMATAIARCAPDEELLSCSSF
SRSGKRRGERMEAQGGKLVCRAHNAFGGEGVYAIARCCLL
PQANCSVHTAPPAEASMGTRVHCHQQGHVLTGCSSHWEVE
DLQPNQCVGHREASIHASCCHAPGLECKVKEHGIPQEQVT
VACEEGWTLTGCSALPSHVLGAYAVDNTCVVRSRAVTAVA
ICCRSR
Description (1)  Proprotein convertase subtilisin/kexin type 9 (E.C.3.4.21.-)


Functional site

1) chain B
residue 328
type
sequence A
description binding site for residue PVV B 801
source : AC1

2) chain B
residue 329
type
sequence S
description binding site for residue PVV B 801
source : AC1

3) chain B
residue 330
type
sequence A
description binding site for residue PVV B 801
source : AC1

4) chain B
residue 331
type
sequence P
description binding site for residue PVV B 801
source : AC1

5) chain B
residue 333
type
sequence V
description binding site for residue PVV B 801
source : AC1

6) chain B
residue 335
type
sequence T
description binding site for residue PVV B 801
source : AC1

7) chain B
residue 357
type
sequence R
description binding site for residue PVV B 801
source : AC1

8) chain B
residue 358
type
sequence C
description binding site for residue PVV B 801
source : AC1

9) chain B
residue 360
type
sequence D
description binding site for residue PVV B 801
source : AC1

10) chain B
residue 458
type
sequence R
description binding site for residue PVV B 801
source : AC1

11) chain B
residue 461
type
sequence W
description binding site for residue PVV B 801
source : AC1

12) chain B
residue 476
type
sequence R
description binding site for residue PVV B 801
source : AC1

13) chain B
residue 533
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16912035
source Swiss-Prot : SWS_FT_FI7

14) chain B
residue 186
type ACT_SITE
sequence D
description Charge relay system => ECO:0000255|PROSITE-ProRule:PRU01240
source Swiss-Prot : SWS_FT_FI1

15) chain B
residue 226
type ACT_SITE
sequence H
description Charge relay system => ECO:0000255|PROSITE-ProRule:PRU01240
source Swiss-Prot : SWS_FT_FI1

16) chain B
residue 386
type ACT_SITE
sequence S
description Charge relay system => ECO:0000255|PROSITE-ProRule:PRU01240
source Swiss-Prot : SWS_FT_FI1


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