eF-site ID 4c6b-A
PDB Code 4c6b
Chain A

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Title Crystal structure of the dihydroorotase domain of human CAD with incomplete active site, obtained recombinantly from E. coli.
Classification HYDROLASE
Compound CAD PROTEIN
Source Homo sapiens (Human) (PYR1_HUMAN)
Sequence A:  KLVRLPGLIDVHVHLREDFASGTAAALAGGITMVCAMPNT
RPPIIDAPALALAQKLAEAGARCDFALFLGASSENAGTLG
TVAGSAAGLKLYLNETFSELRLDSVVQWMEHFETWPSHLP
IVAHAEQQTVAAVLMVAQLTQRSVHICHVARKEEILLIKA
AKARGLPVTCEVAPHHLFLSHDDGEVRPELGSRQDVEALW
ENMAVIDCFASDHAPHTLEEKCRPPPGFPGLETMLPLLLT
AVSEGRLSLDDLLQRLHHNPRRIFHLPPQEDTYVEVDLEH
EWTIPSHMPFSKAHWTPFEGQKVKGTVRRVVLRGEVAYID
GQVLVPPGYGQDVRKWPQGAVPQLPPSPERPRR
Description


Functional site

1) chain A
residue 1586
type
sequence P
description BINDING SITE FOR RESIDUE FMT A 2824
source : AC1

2) chain A
residue 1587
type
sequence I
description BINDING SITE FOR RESIDUE FMT A 2824
source : AC1

3) chain A
residue 1608
type
sequence R
description BINDING SITE FOR RESIDUE FMT A 2824
source : AC1

4) chain A
residue 1609
type
sequence S
description BINDING SITE FOR RESIDUE FMT A 2824
source : AC1

5) chain A
residue 1610
type
sequence V
description BINDING SITE FOR RESIDUE FMT A 2824
source : AC1

6) chain A
residue 1611
type
sequence H
description BINDING SITE FOR RESIDUE FMT A 2824
source : AC1

7) chain A
residue 1734
type
sequence H
description BINDING SITE FOR RESIDUE FMT A 2825
source : AC2

8) chain A
residue 1734
type
sequence H
description BINDING SITE FOR RESIDUE FMT A 2825
source : AC2

9) chain A
residue 1737
type
sequence R
description BINDING SITE FOR RESIDUE FMT A 2825
source : AC2

10) chain A
residue 1737
type
sequence R
description BINDING SITE FOR RESIDUE FMT A 2825
source : AC2

11) chain A
residue 1584
type
sequence H
description BINDING SITE FOR RESIDUE FMT A 2826
source : AC3

12) chain A
residue 1819
type
sequence Q
description BINDING SITE FOR RESIDUE FMT A 2826
source : AC3

13) chain A
residue 1820
type
sequence L
description BINDING SITE FOR RESIDUE FMT A 2826
source : AC3

14) chain A
residue 1604
type
sequence Q
description BINDING SITE FOR RESIDUE FMT A 2827
source : AC4

15) chain A
residue 1605
type
sequence L
description BINDING SITE FOR RESIDUE FMT A 2827
source : AC4

16) chain A
residue 1630
type
sequence R
description BINDING SITE FOR RESIDUE FMT A 2827
source : AC4

17) chain A
residue 1539
type
sequence S
description BINDING SITE FOR RESIDUE FMT A 2828
source : AC5

18) chain A
residue 1540
type
sequence E
description BINDING SITE FOR RESIDUE FMT A 2828
source : AC5

19) chain A
residue 1542
type
sequence A
description BINDING SITE FOR RESIDUE FMT A 2828
source : AC5

20) chain A
residue 1807
type
sequence Q
description BINDING SITE FOR RESIDUE GOL A 2829
source : AC6

21) chain A
residue 1812
type
sequence W
description BINDING SITE FOR RESIDUE GOL A 2829
source : AC6

22) chain A
residue 1814
type
sequence Q
description BINDING SITE FOR RESIDUE GOL A 2829
source : AC6

23) chain A
residue 1684-1695
type prosite
sequence ASDHAPHTLEEK
description DIHYDROOROTASE_2 Dihydroorotase signature 2. ASDhAPHtleeK
source prosite : PS00483

24) chain A
residue 1556
type MOD_RES
sequence K
description N6-carboxylysine => ECO:0000269|PubMed:24332717
source Swiss-Prot : SWS_FT_FI5

25) chain A
residue 1686
type ACT_SITE
sequence D
description For DHOase activity => ECO:0000250|UniProtKB:P05020
source Swiss-Prot : SWS_FT_FI1

26) chain A
residue 1614
type BINDING
sequence H
description BINDING => ECO:0000269|PubMed:24332717, ECO:0007744|PDB:4C6D
source Swiss-Prot : SWS_FT_FI2

27) chain A
residue 1637
type BINDING
sequence E
description BINDING => ECO:0000269|PubMed:24332717, ECO:0007744|PDB:4C6D
source Swiss-Prot : SWS_FT_FI2

28) chain A
residue 1686
type BINDING
sequence D
description BINDING => ECO:0000269|PubMed:24332717, ECO:0007744|PDB:4C6D
source Swiss-Prot : SWS_FT_FI2

29) chain A
residue 1471
type BINDING
sequence H
description BINDING => ECO:0000269|PubMed:24332717, ECO:0007744|PDB:4C6D
source Swiss-Prot : SWS_FT_FI2

30) chain A
residue 1473
type BINDING
sequence H
description BINDING => ECO:0000269|PubMed:24332717, ECO:0007744|PDB:4C6D
source Swiss-Prot : SWS_FT_FI2

31) chain A
residue 1590
type BINDING
sequence H
description BINDING => ECO:0000269|PubMed:24332717, ECO:0007744|PDB:4C6D
source Swiss-Prot : SWS_FT_FI2

32) chain A
residue 1613
type BINDING
sequence C
description BINDING => ECO:0000269|PubMed:24332717, ECO:0007744|PDB:4C6D
source Swiss-Prot : SWS_FT_FI2

33) chain A
residue 1505
type BINDING
sequence N
description BINDING => ECO:0000269|PubMed:24332717, ECO:0007744|PDB:4C6Q
source Swiss-Prot : SWS_FT_FI3

34) chain A
residue 1661
type BINDING
sequence R
description BINDING => ECO:0000269|PubMed:24332717, ECO:0007744|PDB:4C6Q
source Swiss-Prot : SWS_FT_FI3

35) chain A
residue 1690
type BINDING
sequence H
description BINDING => ECO:0000269|PubMed:24332717, ECO:0007744|PDB:4C6Q
source Swiss-Prot : SWS_FT_FI3

36) chain A
residue 1702
type BINDING
sequence P
description BINDING => ECO:0000269|PubMed:24332717, ECO:0007744|PDB:4C6Q
source Swiss-Prot : SWS_FT_FI3

37) chain A
residue 1475
type BINDING
sequence R
description BINDING => ECO:0000269|PubMed:24332717, ECO:0007744|PDB:4C6Q
source Swiss-Prot : SWS_FT_FI3

38) chain A
residue 1556
type BINDING
sequence K
description via carbamate group => ECO:0000269|PubMed:24332717, ECO:0007744|PDB:4C6D
source Swiss-Prot : SWS_FT_FI4


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