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

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Title CRYSTAL STRUCTURE OF THE COMPLEX BETWEEN THE LEECH CARBOXYPEPTIDASE INHIBITOR AND THE HUMAN CARBOXYPEPTIDASE A2 (LCI-CPA2)
Classification HYDROLASE/HYDROLASE INHIBITOR
Compound CARBOXYPEPTIDASE A2
Source ORGANISM_COMMON: human; ORGANISM_SCIENTIFIC: Homo sapiens;
Sequence A:  FNFGAYHTLEEISQEMDNLVAEHPGLVSKVNIGSSFENRP
MNVLKFSTGGDKPAIWLDAGIHAREWVTQATALWTANKIV
SDYGKDPSITSILDALDIFLLPVTNPDGYVFSQTKNRMWR
KTRSKVSAGSLCVGVDPNRNWDAGFGGPGASSNPCSDSYH
GPSANSEVEVKSIVDFIKSHGKVKAFIILHSYSQLLMFPY
GYKCTKLDDFDELSEVAQKAAQSLSRLHGTKYKVGPICSV
IYQASGGSIDWSYDYGIKYSFAFELRDTGRYGFLLPARQI
LPTAEETWLGLKAIMEHVRDHPY
Description (1)  CARBOXYPEPTIDASE A2 (E.C.3.4.15.1) / INHIBITOR COMPLEX


Functional site

1) chain A
residue 424
type
sequence H
description BINDING SITE FOR RESIDUE ZN A 301
source : AC1

2) chain A
residue 427
type
sequence E
description BINDING SITE FOR RESIDUE ZN A 301
source : AC1

3) chain A
residue 552
type
sequence H
description BINDING SITE FOR RESIDUE ZN A 301
source : AC1

4) chain A
residue 424
type
sequence H
description BINDING SITE FOR RESIDUE GLU A 300
source : AC2

5) chain A
residue 482
type
sequence R
description BINDING SITE FOR RESIDUE GLU A 300
source : AC2

6) chain A
residue 500
type
sequence N
description BINDING SITE FOR RESIDUE GLU A 300
source : AC2

7) chain A
residue 501
type
sequence R
description BINDING SITE FOR RESIDUE GLU A 300
source : AC2

8) chain A
residue 552
type
sequence H
description BINDING SITE FOR RESIDUE GLU A 300
source : AC2

9) chain A
residue 604
type
sequence Y
description BINDING SITE FOR RESIDUE GLU A 300
source : AC2

10) chain A
residue 606
type
sequence A
description BINDING SITE FOR RESIDUE GLU A 300
source : AC2

11) chain A
residue 626
type
sequence E
description BINDING SITE FOR RESIDUE GLU A 300
source : AC2

12) chain A
residue 482
type BINDING
sequence R
description BINDING => ECO:0000250|UniProtKB:P00730
source Swiss-Prot : SWS_FT_FI3

13) chain A
residue 500
type BINDING
sequence N
description BINDING => ECO:0000250|UniProtKB:P00730
source Swiss-Prot : SWS_FT_FI3

14) chain A
residue 553
type BINDING
sequence S
description BINDING => ECO:0000250|UniProtKB:P00730
source Swiss-Prot : SWS_FT_FI3

15) chain A
residue 604
type BINDING
sequence Y
description BINDING => ECO:0000250|UniProtKB:P00730
source Swiss-Prot : SWS_FT_FI3

16) chain A
residue 415-437
type prosite
sequence PAIWLDAGIHAREWVTQATALWT
description CARBOXYPEPT_ZN_1 Zinc carboxypeptidases, zinc-binding region 1 signature. PaIwLdaGiHArEwVTQatalwT
source prosite : PS00132

17) chain A
residue 552-562
type prosite
sequence HSYSQLLMFPY
description CARBOXYPEPT_ZN_2 Zinc carboxypeptidases, zinc-binding region 2 signature. HSYSQLLmFPY
source prosite : PS00133

18) chain A
residue 424
type BINDING
sequence H
description BINDING => ECO:0000255|PROSITE-ProRule:PRU01379, ECO:0000269|PubMed:10742178, ECO:0000269|PubMed:9384570
source Swiss-Prot : SWS_FT_FI2

19) chain A
residue 427
type BINDING
sequence E
description BINDING => ECO:0000255|PROSITE-ProRule:PRU01379, ECO:0000269|PubMed:10742178, ECO:0000269|PubMed:9384570
source Swiss-Prot : SWS_FT_FI2

20) chain A
residue 552
type BINDING
sequence H
description BINDING => ECO:0000255|PROSITE-ProRule:PRU01379, ECO:0000269|PubMed:10742178, ECO:0000269|PubMed:9384570
source Swiss-Prot : SWS_FT_FI2


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