eF-site ID 1f8s-G
PDB Code 1f8s
Chain G

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Title CRYSTAL STRUCTURE OF L-AMINO ACID OXIDASE FROM CALLOSELASMA RHODOSTOMA, COMPLEXED WITH THREE MOLECULES OF O-AMINOBENZOATE.
Classification OXIDOREDUCTASE
Compound L-AMINO ACID OXIDASE
Source ORGANISM_COMMON: Malayan pit viper; ORGANISM_SCIENTIFIC: Calloselasma rhodostoma;
Sequence G:  NPLAECFQENDYEEFLEIARNGLKATSNPKHVVIVGAGMA
GLSAAYVLAGAGHQVTVLEASERPGGRVRTYRNEEAGWYA
NLGPMRLPEKHRIVREYIRKFDLRLNEFSQENDNAWYFIK
NIRKKVGEVKKDPGLLKYPVKPSEAGKSAGQLYEESLGKV
VEELKRTNCSYILNKYDTYSTKEYLIKEGDLSPGAVDMIG
DLLNEDSGYYVSFIESLKHDDIFAYEKRFDEIVDGMDKLP
TAMYRDIQDKVHFNAQVIKIQQNDQKVTVVYETLSKETPS
VTADYVIVCTTSRAVRLIKFNPPLLPKKAHALRSVHYRSG
TKIFLTCTTKFWEDDGIHGGKSTTDLPSRFIYYPNHNFTN
GVGVIIAYGIGDDANFFQALDFKDCADIVFNDLSLIHQLP
KKDIQSFCYPSVIQKWSLDKYAMGGITTFTPYQFQHFSDP
LTASQGRIYFAGEYTAQAHGWIDSTIKSGLRAARDVNLAS
EN
Description


Functional site

1) chain G
residue 223
type catalytic
sequence H
description 555
source MCSA : MCSA7

2) chain G
residue 326
type catalytic
sequence K
description 555
source MCSA : MCSA7

3) chain G
residue 43
type BINDING
sequence M
description BINDING => ECO:0000269|PubMed:10944103, ECO:0000269|PubMed:17046020
source Swiss-Prot : SWS_FT_FI1

4) chain G
residue 63
type BINDING
sequence E
description BINDING => ECO:0000269|PubMed:10944103, ECO:0000269|PubMed:17046020
source Swiss-Prot : SWS_FT_FI1

5) chain G
residue 71
type BINDING
sequence R
description BINDING => ECO:0000269|PubMed:10944103, ECO:0000269|PubMed:17046020
source Swiss-Prot : SWS_FT_FI1

6) chain G
residue 87
type BINDING
sequence G
description BINDING => ECO:0000269|PubMed:10944103, ECO:0000269|PubMed:17046020
source Swiss-Prot : SWS_FT_FI1

7) chain G
residue 261
type BINDING
sequence V
description BINDING => ECO:0000269|PubMed:10944103, ECO:0000269|PubMed:17046020
source Swiss-Prot : SWS_FT_FI1

8) chain G
residue 457
type BINDING
sequence E
description BINDING => ECO:0000269|PubMed:10944103, ECO:0000269|PubMed:17046020
source Swiss-Prot : SWS_FT_FI1

9) chain G
residue 90
type BINDING
sequence R
description BINDING => ECO:0000269|PubMed:17046020, ECO:0007744|PDB:1F8R, ECO:0007744|PDB:1F8S, ECO:0007744|PDB:2IID
source Swiss-Prot : SWS_FT_FI2

10) chain G
residue 223
type BINDING
sequence H
description BINDING => ECO:0000269|PubMed:17046020, ECO:0007744|PDB:1F8R, ECO:0007744|PDB:1F8S, ECO:0007744|PDB:2IID
source Swiss-Prot : SWS_FT_FI2

11) chain G
residue 372
type BINDING
sequence Y
description BINDING => ECO:0000269|PubMed:17046020, ECO:0007744|PDB:1F8R, ECO:0007744|PDB:1F8S, ECO:0007744|PDB:2IID
source Swiss-Prot : SWS_FT_FI2

12) chain G
residue 464
type BINDING
sequence G
description BINDING => ECO:0000269|PubMed:17046020, ECO:0007744|PDB:1F8S, ECO:0007744|PDB:2IID
source Swiss-Prot : SWS_FT_FI3

13) chain G
residue 172
type CARBOHYD
sequence N
description N-linked (GlcNAc...) (complex) asparagine => ECO:0000269|PubMed:10944103, ECO:0000269|PubMed:11453999
source Swiss-Prot : SWS_FT_FI4

14) chain G
residue 361
type CARBOHYD
sequence N
description N-linked (GlcNAc...) (complex) asparagine => ECO:0000269|PubMed:10944103, ECO:0000269|PubMed:11453999
source Swiss-Prot : SWS_FT_FI4


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