eF-site ID 4pxe-AB
PDB Code 4pxe
Chain A, B

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Title The crystal structure of AtUAH in complex with glyoxylate
Classification HYDROLASE
Compound Ureidoglycolate hydrolase
Source Arabidopsis thaliana (Mouse-ear cress) (UAH_ARATH)
Sequence A:  NLASSLSVDAPGLQNQIDELSSFSDAPSPSVTRVLYTDKD
VSARRYVKNLMALAGLTVREDAVGNIFGKWDGLEPNLPAV
ATGSHIDAIPYSGKYDGVVGVLGAIEAINVLKRSGFKPKR
SLEIILFTSEEPTRFGISCLGSRLLAGSKELAEALKTTVV
DGQNVSFIEAARSAGYAEDKDDDLSSVFLKKGSYFAFLEL
HIEQGPILEDEGLDIGVVTAIAAPASLKVEFEGNGGHAGA
VLMPYRNDAGLAAAELALAVEKHVLESESIDTVGTVGILE
LHPGAINSIPSKSHLEIDTRDIDEARRNTVIKKIQESANT
IAKKRKVKLSEFKIVNQDPPALSDKLVIKKMAEAATELNL
SHKMMISRAYHDSLFMARISPMGMIFIPCYKGYSHKPEEY
SSPEDMANGVKVLSLTLAKLSLD
B:  NLASSLSVDAPGLQNQIDELSSFSDAPSPSVTRVLYTDKD
VSARRYVKNLMALAGLTVREDAVGNIFGKWDGLEPNLPAV
ATGSHIDAIPYSGKYDGVVGVLGAIEAINVLKRSGFKPKR
SLEIILFTSEEPTRFGISCLGSRLLAGSKELAEALKTTVV
DGQNVSFIEAARSAGYAEDKDDDLSSVFLKKGSYFAFLEL
HIEQGPILEDEGLDIGVVTAIAAPASLKVEFEGNGGHAGA
VLMPYRNDAGLAAAELALAVEKHVLESESIDTVGTVGILE
LHPGAINSIPSKSHLEIDTRDIDEARRNTVIKKIQESANT
IAKKRKVKLSEFKIVNQDPPALSDKLVIKKMAEAATELNL
SHKMMISRAYHDSLFMARISPMGMIFIPCYKGYSHKPEEY
SSPEDMANGVKVLSLTLAKLSLD
Description


Functional site
1) chain A
residue 138
type
sequence H
description BINDING SITE FOR RESIDUE MN A 501
source : AC1
2) chain A
residue 149
type
sequence D
description BINDING SITE FOR RESIDUE MN A 501
source : AC1
3) chain A
residue 254
type
sequence H
description BINDING SITE FOR RESIDUE MN A 501
source : AC1
4) chain A
residue 149
type
sequence D
description BINDING SITE FOR RESIDUE MN A 502
source : AC2
5) chain A
residue 184
type
sequence E
description BINDING SITE FOR RESIDUE MN A 502
source : AC2
6) chain A
residue 448
type
sequence H
description BINDING SITE FOR RESIDUE MN A 502
source : AC2
7) chain A
residue 183
type
sequence E
description BINDING SITE FOR RESIDUE GLV A 503
source : AC3
8) chain A
residue 184
type
sequence E
description BINDING SITE FOR RESIDUE GLV A 503
source : AC3
9) chain A
residue 353
type
sequence R
description BINDING SITE FOR RESIDUE GLV A 503
source : AC3
10) chain A
residue 422
type
sequence A
description BINDING SITE FOR RESIDUE GLV A 503
source : AC3
11) chain A
residue 423
type
sequence Y
description BINDING SITE FOR RESIDUE GLV A 503
source : AC3
12) chain A
residue 448
type
sequence H
description BINDING SITE FOR RESIDUE GLV A 503
source : AC3
13) chain B
residue 290
type
sequence H
description BINDING SITE FOR RESIDUE GLV A 503
source : AC3
14) chain B
residue 340
type
sequence N
description BINDING SITE FOR RESIDUE GLV A 503
source : AC3
15) chain B
residue 138
type
sequence H
description BINDING SITE FOR RESIDUE MN B 501
source : AC4
16) chain B
residue 149
type
sequence D
description BINDING SITE FOR RESIDUE MN B 501
source : AC4
17) chain B
residue 254
type
sequence H
description BINDING SITE FOR RESIDUE MN B 501
source : AC4
18) chain B
residue 149
type
sequence D
description BINDING SITE FOR RESIDUE MN B 502
source : AC5
19) chain B
residue 184
type
sequence E
description BINDING SITE FOR RESIDUE MN B 502
source : AC5
20) chain B
residue 448
type
sequence H
description BINDING SITE FOR RESIDUE MN B 502
source : AC5
21) chain A
residue 290
type
sequence H
description BINDING SITE FOR RESIDUE GLV B 503
source : AC6
22) chain A
residue 340
type
sequence N
description BINDING SITE FOR RESIDUE GLV B 503
source : AC6
23) chain B
residue 183
type
sequence E
description BINDING SITE FOR RESIDUE GLV B 503
source : AC6
24) chain B
residue 184
type
sequence E
description BINDING SITE FOR RESIDUE GLV B 503
source : AC6
25) chain B
residue 353
type
sequence R
description BINDING SITE FOR RESIDUE GLV B 503
source : AC6
26) chain B
residue 422
type
sequence A
description BINDING SITE FOR RESIDUE GLV B 503
source : AC6
27) chain B
residue 423
type
sequence Y
description BINDING SITE FOR RESIDUE GLV B 503
source : AC6
28) chain B
residue 448
type
sequence H
description BINDING SITE FOR RESIDUE GLV B 503
source : AC6
29) chain A
residue 299
type SITE
sequence R
description Necessary for dimerization => ECO:0000250|UniProtKB:Q53389
source Swiss-Prot : SWS_FT_FI4
30) chain B
residue 299
type SITE
sequence R
description Necessary for dimerization => ECO:0000250|UniProtKB:Q53389
source Swiss-Prot : SWS_FT_FI4
31) chain A
residue 138
type BINDING
sequence H
description BINDING => ECO:0000269|PubMed:25020232, ECO:0007744|PDB:4PXB, ECO:0007744|PDB:4PXC, ECO:0007744|PDB:4PXE
source Swiss-Prot : SWS_FT_FI1
32) chain B
residue 149
type BINDING
sequence D
description BINDING => ECO:0000269|PubMed:25020232, ECO:0007744|PDB:4PXB, ECO:0007744|PDB:4PXC, ECO:0007744|PDB:4PXE
source Swiss-Prot : SWS_FT_FI1
33) chain B
residue 183
type BINDING
sequence E
description BINDING => ECO:0000269|PubMed:25020232, ECO:0007744|PDB:4PXB, ECO:0007744|PDB:4PXC, ECO:0007744|PDB:4PXE
source Swiss-Prot : SWS_FT_FI1
34) chain B
residue 184
type BINDING
sequence E
description BINDING => ECO:0000269|PubMed:25020232, ECO:0007744|PDB:4PXB, ECO:0007744|PDB:4PXC, ECO:0007744|PDB:4PXE
source Swiss-Prot : SWS_FT_FI1
35) chain B
residue 254
type BINDING
sequence H
description BINDING => ECO:0000269|PubMed:25020232, ECO:0007744|PDB:4PXB, ECO:0007744|PDB:4PXC, ECO:0007744|PDB:4PXE
source Swiss-Prot : SWS_FT_FI1
36) chain B
residue 340
type BINDING
sequence N
description BINDING => ECO:0000269|PubMed:25020232, ECO:0007744|PDB:4PXB, ECO:0007744|PDB:4PXC, ECO:0007744|PDB:4PXE
source Swiss-Prot : SWS_FT_FI1
37) chain B
residue 353
type BINDING
sequence R
description BINDING => ECO:0000269|PubMed:25020232, ECO:0007744|PDB:4PXB, ECO:0007744|PDB:4PXC, ECO:0007744|PDB:4PXE
source Swiss-Prot : SWS_FT_FI1
38) chain B
residue 423
type BINDING
sequence Y
description BINDING => ECO:0000269|PubMed:25020232, ECO:0007744|PDB:4PXB, ECO:0007744|PDB:4PXC, ECO:0007744|PDB:4PXE
source Swiss-Prot : SWS_FT_FI1
39) chain A
residue 149
type BINDING
sequence D
description BINDING => ECO:0000269|PubMed:25020232, ECO:0007744|PDB:4PXB, ECO:0007744|PDB:4PXC, ECO:0007744|PDB:4PXE
source Swiss-Prot : SWS_FT_FI1
40) chain A
residue 183
type BINDING
sequence E
description BINDING => ECO:0000269|PubMed:25020232, ECO:0007744|PDB:4PXB, ECO:0007744|PDB:4PXC, ECO:0007744|PDB:4PXE
source Swiss-Prot : SWS_FT_FI1
41) chain A
residue 184
type BINDING
sequence E
description BINDING => ECO:0000269|PubMed:25020232, ECO:0007744|PDB:4PXB, ECO:0007744|PDB:4PXC, ECO:0007744|PDB:4PXE
source Swiss-Prot : SWS_FT_FI1
42) chain A
residue 254
type BINDING
sequence H
description BINDING => ECO:0000269|PubMed:25020232, ECO:0007744|PDB:4PXB, ECO:0007744|PDB:4PXC, ECO:0007744|PDB:4PXE
source Swiss-Prot : SWS_FT_FI1
43) chain A
residue 340
type BINDING
sequence N
description BINDING => ECO:0000269|PubMed:25020232, ECO:0007744|PDB:4PXB, ECO:0007744|PDB:4PXC, ECO:0007744|PDB:4PXE
source Swiss-Prot : SWS_FT_FI1
44) chain A
residue 353
type BINDING
sequence R
description BINDING => ECO:0000269|PubMed:25020232, ECO:0007744|PDB:4PXB, ECO:0007744|PDB:4PXC, ECO:0007744|PDB:4PXE
source Swiss-Prot : SWS_FT_FI1
45) chain A
residue 423
type BINDING
sequence Y
description BINDING => ECO:0000269|PubMed:25020232, ECO:0007744|PDB:4PXB, ECO:0007744|PDB:4PXC, ECO:0007744|PDB:4PXE
source Swiss-Prot : SWS_FT_FI1
46) chain B
residue 138
type BINDING
sequence H
description BINDING => ECO:0000269|PubMed:25020232, ECO:0007744|PDB:4PXB, ECO:0007744|PDB:4PXC, ECO:0007744|PDB:4PXE
source Swiss-Prot : SWS_FT_FI1
47) chain A
residue 290
type BINDING
sequence H
description BINDING => ECO:0000269|PubMed:25020232, ECO:0007744|PDB:4PXB
source Swiss-Prot : SWS_FT_FI2
48) chain B
residue 290
type BINDING
sequence H
description BINDING => ECO:0000269|PubMed:25020232, ECO:0007744|PDB:4PXB
source Swiss-Prot : SWS_FT_FI2
49) chain A
residue 448
type BINDING
sequence H
description BINDING => ECO:0000269|PubMed:25020232, ECO:0007744|PDB:4PXB, ECO:0007744|PDB:4PXC
source Swiss-Prot : SWS_FT_FI3
50) chain B
residue 448
type BINDING
sequence H
description BINDING => ECO:0000269|PubMed:25020232, ECO:0007744|PDB:4PXB, ECO:0007744|PDB:4PXC
source Swiss-Prot : SWS_FT_FI3

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