eF-site ID 1cg2-B
PDB Code 1cg2
Chain B

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Title CARBOXYPEPTIDASE G2
Classification METALLOCARBOXYPEPTIDASE
Compound CARBOXYPEPTIDASE G2
Source null (CBPG_PSES6)
Sequence B:  QKRDNVLFQAATDEQPAVIKTLEKLVNIETGTGDAEGIAA
AGNFLEAELKNLGFTVTRSKSAGLVVGDNIVGKIKGRGGK
NLLLMSHMDTVYLKGILAKAPFRVEGDKAYGPGIADDKGG
NAVILHTLKLLKEYGVRDYGTITVLFNTDEEKGSFGSRDL
IQEEAKLADYVLSFEPTSAGDEKLSLGTSGIAYVQVNITG
KASHAGAAPELGVNALVEASDLVLRTMNIDDKAKNLRFNW
TIAKAGNVSNIIPASATLNADVRYARNEDFDAAMKTLEER
AQQKKLPEADVKVIVTRGRPAFNAGEGGKKLVDKAVAYYK
EAGGTLGVEERTGGGTDAAYAALSGKPVIESLGLPGFGYH
SDKAEYVDISAIPRRLYMAARLIMDLGAG
Description


Functional site

1) chain B
residue 112
type
sequence H
description CATALYTIC SITE.
source : CTB

2) chain B
residue 141
type
sequence D
description CATALYTIC SITE.
source : CTB

3) chain B
residue 176
type
sequence E
description CATALYTIC SITE.
source : CTB

4) chain B
residue 200
type
sequence E
description CATALYTIC SITE.
source : CTB

5) chain B
residue 385
type
sequence H
description CATALYTIC SITE.
source : CTB

6) chain B
residue 141
type
sequence D
description BINDING SITE FOR RESIDUE ZN B 500
source : AC5

7) chain B
residue 176
type
sequence E
description BINDING SITE FOR RESIDUE ZN B 500
source : AC5

8) chain B
residue 385
type
sequence H
description BINDING SITE FOR RESIDUE ZN B 500
source : AC5

9) chain B
residue 112
type
sequence H
description BINDING SITE FOR RESIDUE ZN B 501
source : AC6

10) chain B
residue 141
type
sequence D
description BINDING SITE FOR RESIDUE ZN B 501
source : AC6

11) chain B
residue 175
type
sequence E
description BINDING SITE FOR RESIDUE ZN B 501
source : AC6

12) chain B
residue 200
type
sequence E
description BINDING SITE FOR RESIDUE ZN B 501
source : AC6

13) chain B
residue 229
type
sequence H
description BINDING SITE FOR RESIDUE ZN B 502
source : AC7

14) chain B
residue 387
type
sequence D
description BINDING SITE FOR RESIDUE ZN D 502
source : BC4

15) chain B
residue 112
type catalytic
sequence H
description 447
source MCSA : MCSA2

16) chain B
residue 141
type catalytic
sequence D
description 447
source MCSA : MCSA2

17) chain B
residue 175
type catalytic
sequence E
description 447
source MCSA : MCSA2

18) chain B
residue 176
type catalytic
sequence E
description 447
source MCSA : MCSA2

19) chain B
residue 200
type catalytic
sequence E
description 447
source MCSA : MCSA2

20) chain B
residue 385
type catalytic
sequence H
description 447
source MCSA : MCSA2

21) chain B
residue 114
type ACT_SITE
sequence D
description ACT_SITE => ECO:0000250
source Swiss-Prot : SWS_FT_FI1

22) chain B
residue 175
type ACT_SITE
sequence E
description Proton acceptor => ECO:0000269|PubMed:9083113
source Swiss-Prot : SWS_FT_FI2

23) chain B
residue 112
type BINDING
sequence H
description BINDING => ECO:0000269|PubMed:9083113
source Swiss-Prot : SWS_FT_FI3

24) chain B
residue 141
type BINDING
sequence D
description BINDING => ECO:0000269|PubMed:9083113
source Swiss-Prot : SWS_FT_FI3

25) chain B
residue 176
type BINDING
sequence E
description BINDING => ECO:0000269|PubMed:9083113
source Swiss-Prot : SWS_FT_FI3

26) chain B
residue 200
type BINDING
sequence E
description BINDING => ECO:0000269|PubMed:9083113
source Swiss-Prot : SWS_FT_FI3

27) chain B
residue 385
type BINDING
sequence H
description BINDING => ECO:0000269|PubMed:9083113
source Swiss-Prot : SWS_FT_FI3


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