eF-site ID 1a2z-ABCD
PDB Code 1a2z
Chain A, B, C, D

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Title PYRROLIDONE CARBOXYL PEPTIDASE FROM THERMOCOCCUS LITORALIS
Classification PEPTIDASE
Compound PYRROLIDONE CARBOXYL PEPTIDASE
Source Thermococcus litoralis (strain ATCC 51850 / DSM 5473 / JCM 8560 / NS-C) (PCP_THELI)
Sequence A:  MKKVLITGFEPFGGDSKNPTEQIAKYFDRKQIGNAMVYGR
VLPVSVKRATIELKRYLEEIKPEIVINLGLAPTYSNITVE
RIAVNIIDARIPDNDGYQPIDEKIEEDAPLAYMATLPVRA
ITKTLRDNGIPATISYSAGTYLCNYVMFKTLHFSKIEGYP
LKAGFIHVPYTPDQVVNKFFLLGKNTPSMCLEAEIKAIEL
AVKVSLDYLEKDRDDIKIPL
B:  MKKVLITGFEPFGGDSKNPTEQIAKYFDRKQIGNAMVYGR
VLPVSVKRATIELKRYLEEIKPEIVINLGLAPTYSNITVE
RIAVNIIDARIPDNDGYQPIDEKIEEDAPLAYMATLPVRA
ITKTLRDNGIPATISYSAGTYLCNYVMFKTLHFSKIEGYP
LKAGFIHVPYTPDQVVNKFFLLGKNTPSMCLEAEIKAIEL
AVKVSLDYLEKDRDDIKIPL
C:  MKKVLITGFEPFGGDSKNPTEQIAKYFDRKQIGNAMVYGR
VLPVSVKRATIELKRYLEEIKPEIVINLGLAPTYSNITVE
RIAVNIIDARIPDNDGYQPIDEKIEEDAPLAYMATLPVRA
ITKTLRDNGIPATISYSAGTYLCNYVMFKTLHFSKIEGYP
LKAGFIHVPYTPDQVVNKFFLLGKNTPSMCLEAEIKAIEL
AVKVSLDYLEKDRDDIKIPL
D:  MKKVLITGFEPFGGDSKNPTEQIAKYFDRKQIGNAMVYGR
VLPVSVKRATIELKRYLEEIKPEIVINLGLAPTYSNITVE
RIAVNIIDARIPDNDGYQPIDEKIEEDAPLAYMATLPVRA
ITKTLRDNGIPATISYSAGTYLCNYVMFKTLHFSKIEGYP
LKAGFIHVPYTPDQVVNKFFLLGKNTPSMCLEAEIKAIEL
AVKVSLDYLEKDRDDIKIPL
Description (1)  PYRROLIDONE CARBOXYL PEPTIDASE


Functional site

1) chain A
residue 80
type
sequence E
description CATALYTIC TRIAD.
source : AVE

2) chain A
residue 143
type
sequence C
description CATALYTIC TRIAD.
source : AVE

3) chain A
residue 167
type
sequence H
description CATALYTIC TRIAD.
source : AVE

4) chain A
residue 1
type
sequence M
description BINDING SITE FOR RESIDUE SO4 A 621
source : AC1

5) chain B
residue 38
type
sequence Y
description BINDING SITE FOR RESIDUE SO4 A 621
source : AC1

6) chain B
residue 1
type
sequence M
description BINDING SITE FOR RESIDUE SO4 B 622
source : AC2

7) chain B
residue 2
type
sequence K
description BINDING SITE FOR RESIDUE SO4 B 622
source : AC2

8) chain B
residue 34
type
sequence N
description BINDING SITE FOR RESIDUE SO4 B 622
source : AC2

9) chain C
residue 1
type
sequence M
description BINDING SITE FOR RESIDUE SO4 C 623
source : AC3

10) chain C
residue 1
type
sequence M
description BINDING SITE FOR RESIDUE SO4 D 624
source : AC4

11) chain D
residue 1
type
sequence M
description BINDING SITE FOR RESIDUE SO4 D 624
source : AC4

12) chain D
residue 2
type
sequence K
description BINDING SITE FOR RESIDUE SO4 D 624
source : AC4

13) chain D
residue 34
type
sequence N
description BINDING SITE FOR RESIDUE SO4 D 624
source : AC4

14) chain A
residue 69-85
type prosite
sequence GLAPTYSNITVERIAVN
description PYRASE_GLU Pyrrolidone-carboxylate peptidase glutamic acid active site. GlaPtysnITvERIAvN
source prosite : PS01333

15) chain A
residue 130-144
type prosite
sequence IPATISYSAGTYLCN
description PYRASE_CYS Pyrrolidone-carboxylate peptidase cysteine active site. IpAtISySAGtYLCN
source prosite : PS01334

16) chain A
residue 80
type ACT_SITE
sequence E
description
source Swiss-Prot : SWS_FT_FI1

17) chain D
residue 80
type ACT_SITE
sequence E
description
source Swiss-Prot : SWS_FT_FI1

18) chain D
residue 143
type ACT_SITE
sequence C
description
source Swiss-Prot : SWS_FT_FI1

19) chain D
residue 167
type ACT_SITE
sequence H
description
source Swiss-Prot : SWS_FT_FI1

20) chain A
residue 143
type ACT_SITE
sequence C
description
source Swiss-Prot : SWS_FT_FI1

21) chain A
residue 167
type ACT_SITE
sequence H
description
source Swiss-Prot : SWS_FT_FI1

22) chain B
residue 80
type ACT_SITE
sequence E
description
source Swiss-Prot : SWS_FT_FI1

23) chain B
residue 143
type ACT_SITE
sequence C
description
source Swiss-Prot : SWS_FT_FI1

24) chain B
residue 167
type ACT_SITE
sequence H
description
source Swiss-Prot : SWS_FT_FI1

25) chain C
residue 80
type ACT_SITE
sequence E
description
source Swiss-Prot : SWS_FT_FI1

26) chain C
residue 143
type ACT_SITE
sequence C
description
source Swiss-Prot : SWS_FT_FI1

27) chain C
residue 167
type ACT_SITE
sequence H
description
source Swiss-Prot : SWS_FT_FI1


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