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

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Title ALTERING THE BINUCLEAR MANGANESE CLUSTER OF ARGINASE DIMINISHES THERMOSTABILITY AND CATALYTIC FUNCTION
Classification HYDROLASE
Compound ARGINASE
Source Rattus norvegicus (Rat) (ARGI1_RAT)
Sequence A:  KPIEIIGAPFSKGQPRGGVEKGPAALRKAGLVEKLKETEY
NVRDHGDLAFVDVPNDSPFQIVKNPRSVGKANEQLAAVVA
ETQKNGTISVVLGGDNSMAIGSISGHARVHPDLCVIWVDA
HTDINTPLTTSSGNLHGQPVAFLLKELKGKFPDVPGFSWV
TPCISAKDIVYIGLRDVDPGEHYIIKTLGIKYFSMTEVDK
LGIGKVMEETFSYLLGRKKRPIHLSFDVDGLDPVFTPATG
TPVVGGLSYREGLYITEEIYKTGLLSGLDIMEVNPTLGKT
PEEVTRTVNTAVALTLSCFGTKREGNHKPETDYL
Description


Functional site

1) chain A
residue 101
type
sequence N
description BI-MANGANESE NUCLEAR BINDING SITE.
source : MNA

2) chain A
residue 124
type
sequence D
description BI-MANGANESE NUCLEAR BINDING SITE.
source : MNA

3) chain A
residue 126
type
sequence H
description BI-MANGANESE NUCLEAR BINDING SITE.
source : MNA

4) chain A
residue 128
type
sequence D
description BI-MANGANESE NUCLEAR BINDING SITE.
source : MNA

5) chain A
residue 232
type
sequence D
description BI-MANGANESE NUCLEAR BINDING SITE.
source : MNA

6) chain A
residue 234
type
sequence D
description BI-MANGANESE NUCLEAR BINDING SITE.
source : MNA

7) chain A
residue 124
type
sequence D
description BINDING SITE FOR RESIDUE MN A 500
source : AC1

8) chain A
residue 126
type
sequence H
description BINDING SITE FOR RESIDUE MN A 500
source : AC1

9) chain A
residue 232
type
sequence D
description BINDING SITE FOR RESIDUE MN A 500
source : AC1

10) chain A
residue 234
type
sequence D
description BINDING SITE FOR RESIDUE MN A 500
source : AC1

11) chain A
residue 281
type MOD_RES
sequence T
description Phosphothreonine => ECO:0007744|PubMed:22673903
source Swiss-Prot : SWS_FT_FI14

12) chain A
residue 124
type BINDING
sequence D
description BINDING => ECO:0000269|PubMed:10542097, ECO:0000269|PubMed:12820884, ECO:0000269|PubMed:15315440, ECO:0000269|PubMed:16266687, ECO:0000269|PubMed:8849731, ECO:0000269|PubMed:9265637, ECO:0007744|PDB:1D3V, ECO:0007744|PDB:1HQ5, ECO:0007744|PDB:1HQF, ECO:0007744|PDB:1HQG, ECO:0007744|PDB:1HQH, ECO:0007744|PDB:1HQX, ECO:0007744|PDB:1P8M, ECO:0007744|PDB:1P8O, ECO:0007744|PDB:1P8P, ECO:0007744|PDB:1P8Q, ECO:0007744|PDB:1P8R, ECO:0007744|PDB:1P8S, ECO:0007744|PDB:1R1O, ECO:0007744|PDB:1RLA, ECO:0007744|PDB:1T4P, ECO:0007744|PDB:1T4R, ECO:0007744|PDB:1T4S, ECO:0007744|PDB:1T4T, ECO:0007744|PDB:1T5F, ECO:0007744|PDB:1T5G, ECO:0007744|PDB:1TA1, ECO:0007744|PDB:1TBH, ECO:0007744|PDB:1TBJ, ECO:0007744|PDB:1TBL, ECO:0007744|PDB:1ZPE, ECO:0007744|PDB:1ZPG, ECO:0007744|PDB:2RLA, ECO:0007744|PDB:3E8Q, ECO:0007744|PDB:3E8Z, ECO:0007744|PDB:3E9B, ECO:0007744|PDB:3RLA, ECO:0007744|PDB:4RLA, ECO:0007744|PDB:5RLA
source Swiss-Prot : SWS_FT_FI2

13) chain A
residue 126
type BINDING
sequence H
description BINDING => ECO:0000269|PubMed:10542097, ECO:0000269|PubMed:12820884, ECO:0000269|PubMed:15315440, ECO:0000269|PubMed:16266687, ECO:0000269|PubMed:8849731, ECO:0000269|PubMed:9265637, ECO:0007744|PDB:1D3V, ECO:0007744|PDB:1HQ5, ECO:0007744|PDB:1HQF, ECO:0007744|PDB:1HQG, ECO:0007744|PDB:1HQH, ECO:0007744|PDB:1HQX, ECO:0007744|PDB:1P8M, ECO:0007744|PDB:1P8O, ECO:0007744|PDB:1P8P, ECO:0007744|PDB:1P8Q, ECO:0007744|PDB:1P8R, ECO:0007744|PDB:1P8S, ECO:0007744|PDB:1R1O, ECO:0007744|PDB:1RLA, ECO:0007744|PDB:1T4P, ECO:0007744|PDB:1T4R, ECO:0007744|PDB:1T4S, ECO:0007744|PDB:1T4T, ECO:0007744|PDB:1T5F, ECO:0007744|PDB:1T5G, ECO:0007744|PDB:1TA1, ECO:0007744|PDB:1TBH, ECO:0007744|PDB:1TBJ, ECO:0007744|PDB:1TBL, ECO:0007744|PDB:1ZPE, ECO:0007744|PDB:1ZPG, ECO:0007744|PDB:2RLA, ECO:0007744|PDB:3E8Q, ECO:0007744|PDB:3E8Z, ECO:0007744|PDB:3E9B, ECO:0007744|PDB:3RLA, ECO:0007744|PDB:4RLA, ECO:0007744|PDB:5RLA
source Swiss-Prot : SWS_FT_FI2

14) chain A
residue 128
type BINDING
sequence D
description BINDING => ECO:0000269|PubMed:10542097, ECO:0000269|PubMed:12820884, ECO:0000269|PubMed:15315440, ECO:0000269|PubMed:16266687, ECO:0000269|PubMed:8849731, ECO:0000269|PubMed:9265637, ECO:0007744|PDB:1D3V, ECO:0007744|PDB:1HQ5, ECO:0007744|PDB:1HQF, ECO:0007744|PDB:1HQG, ECO:0007744|PDB:1HQH, ECO:0007744|PDB:1HQX, ECO:0007744|PDB:1P8N, ECO:0007744|PDB:1P8P, ECO:0007744|PDB:1P8Q, ECO:0007744|PDB:1P8R, ECO:0007744|PDB:1P8S, ECO:0007744|PDB:1R1O, ECO:0007744|PDB:1RLA, ECO:0007744|PDB:1T4P, ECO:0007744|PDB:1T4R, ECO:0007744|PDB:1T4S, ECO:0007744|PDB:1T4T, ECO:0007744|PDB:1T5F, ECO:0007744|PDB:1T5G, ECO:0007744|PDB:1TA1, ECO:0007744|PDB:1TBH, ECO:0007744|PDB:1TBJ, ECO:0007744|PDB:1TBL, ECO:0007744|PDB:1ZPE, ECO:0007744|PDB:1ZPG, ECO:0007744|PDB:3E8Q, ECO:0007744|PDB:3E8Z, ECO:0007744|PDB:3E9B, ECO:0007744|PDB:3RLA
source Swiss-Prot : SWS_FT_FI3

15) chain A
residue 232
type BINDING
sequence D
description BINDING => ECO:0000269|PubMed:10542097, ECO:0000269|PubMed:12820884, ECO:0000269|PubMed:15315440, ECO:0000269|PubMed:16266687, ECO:0000269|PubMed:8849731, ECO:0000269|PubMed:9265637, ECO:0007744|PDB:1D3V, ECO:0007744|PDB:1HQ5, ECO:0007744|PDB:1HQF, ECO:0007744|PDB:1HQG, ECO:0007744|PDB:1HQH, ECO:0007744|PDB:1HQX, ECO:0007744|PDB:1P8M, ECO:0007744|PDB:1P8O, ECO:0007744|PDB:1P8P, ECO:0007744|PDB:1P8Q, ECO:0007744|PDB:1P8R, ECO:0007744|PDB:1R1O, ECO:0007744|PDB:1RLA, ECO:0007744|PDB:1T4P, ECO:0007744|PDB:1T4R, ECO:0007744|PDB:1T4S, ECO:0007744|PDB:1T4T, ECO:0007744|PDB:1T5F, ECO:0007744|PDB:1T5G, ECO:0007744|PDB:1TA1, ECO:0007744|PDB:1TBH, ECO:0007744|PDB:1TBJ, ECO:0007744|PDB:1TBL, ECO:0007744|PDB:1ZPE, ECO:0007744|PDB:1ZPG, ECO:0007744|PDB:2RLA, ECO:0007744|PDB:3E8Q, ECO:0007744|PDB:3E8Z, ECO:0007744|PDB:3E9B, ECO:0007744|PDB:3RLA, ECO:0007744|PDB:4RLA, ECO:0007744|PDB:5RLA
source Swiss-Prot : SWS_FT_FI6

16) chain A
residue 234
type BINDING
sequence D
description BINDING => ECO:0000269|PubMed:10542097, ECO:0000269|PubMed:12820884, ECO:0000269|PubMed:15315440, ECO:0000269|PubMed:16266687, ECO:0000269|PubMed:8849731, ECO:0000269|PubMed:9265637, ECO:0007744|PDB:1D3V, ECO:0007744|PDB:1HQ5, ECO:0007744|PDB:1HQF, ECO:0007744|PDB:1HQG, ECO:0007744|PDB:1HQH, ECO:0007744|PDB:1HQX, ECO:0007744|PDB:1P8M, ECO:0007744|PDB:1P8O, ECO:0007744|PDB:1P8P, ECO:0007744|PDB:1P8R, ECO:0007744|PDB:1P8S, ECO:0007744|PDB:1R1O, ECO:0007744|PDB:1RLA, ECO:0007744|PDB:1T4P, ECO:0007744|PDB:1T4R, ECO:0007744|PDB:1T4S, ECO:0007744|PDB:1T4T, ECO:0007744|PDB:1T5F, ECO:0007744|PDB:1T5G, ECO:0007744|PDB:1TA1, ECO:0007744|PDB:1TBH, ECO:0007744|PDB:1TBJ, ECO:0007744|PDB:1TBL, ECO:0007744|PDB:1ZPE, ECO:0007744|PDB:1ZPG, ECO:0007744|PDB:2RLA, ECO:0007744|PDB:3E8Q, ECO:0007744|PDB:3E8Z, ECO:0007744|PDB:3E9B, ECO:0007744|PDB:3RLA, ECO:0007744|PDB:4RLA, ECO:0007744|PDB:5RLA
source Swiss-Prot : SWS_FT_FI7

17) chain A
residue 246
type BINDING
sequence T
description BINDING => ECO:0000250|UniProtKB:P53608
source Swiss-Prot : SWS_FT_FI8

18) chain A
residue 277
type BINDING
sequence E
description BINDING => ECO:0000250|UniProtKB:P78540
source Swiss-Prot : SWS_FT_FI9

19) chain A
residue 17
type MOD_RES
sequence K
description N6-succinyllysine => ECO:0000250|UniProtKB:Q61176
source Swiss-Prot : SWS_FT_FI10

20) chain A
residue 75
type MOD_RES
sequence K
description N6-succinyllysine => ECO:0000250|UniProtKB:Q61176
source Swiss-Prot : SWS_FT_FI10

21) chain A
residue 62
type MOD_RES
sequence S
description Phosphoserine => ECO:0007744|PubMed:22673903
source Swiss-Prot : SWS_FT_FI11

22) chain A
residue 72
type MOD_RES
sequence S
description Phosphoserine => ECO:0000250|UniProtKB:Q61176
source Swiss-Prot : SWS_FT_FI12

23) chain A
residue 163
type MOD_RES
sequence S
description Phosphoserine => ECO:0000250|UniProtKB:P05089
source Swiss-Prot : SWS_FT_FI13

24) chain A
residue 217
type MOD_RES
sequence S
description Phosphoserine => ECO:0000250|UniProtKB:P05089
source Swiss-Prot : SWS_FT_FI13

25) chain A
residue 101
type BINDING
sequence N
description BINDING => ECO:0000269|PubMed:10542097, ECO:0000269|PubMed:12820884, ECO:0000269|PubMed:15315440, ECO:0000269|PubMed:16266687, ECO:0000269|PubMed:8849731, ECO:0007744|PDB:1D3V, ECO:0007744|PDB:1HQ5, ECO:0007744|PDB:1HQF, ECO:0007744|PDB:1HQG, ECO:0007744|PDB:1HQH, ECO:0007744|PDB:1HQX, ECO:0007744|PDB:1P8M, ECO:0007744|PDB:1P8N, ECO:0007744|PDB:1P8O, ECO:0007744|PDB:1P8Q, ECO:0007744|PDB:1P8S, ECO:0007744|PDB:1R1O, ECO:0007744|PDB:1RLA, ECO:0007744|PDB:1T4P, ECO:0007744|PDB:1T4R, ECO:0007744|PDB:1T4S, ECO:0007744|PDB:1T4T, ECO:0007744|PDB:1T5F, ECO:0007744|PDB:1T5G, ECO:0007744|PDB:1TA1, ECO:0007744|PDB:1TBH, ECO:0007744|PDB:1TBJ, ECO:0007744|PDB:1TBL, ECO:0007744|PDB:1ZPE, ECO:0007744|PDB:1ZPG, ECO:0007744|PDB:3E8Q, ECO:0007744|PDB:3E8Z, ECO:0007744|PDB:3E9B
source Swiss-Prot : SWS_FT_FI1

26) chain A
residue 137
type BINDING
sequence S
description BINDING => ECO:0007744|PDB:1HQG, ECO:0007744|PDB:1HQH
source Swiss-Prot : SWS_FT_FI4

27) chain A
residue 183
type BINDING
sequence D
description BINDING => ECO:0007744|PDB:1T5G
source Swiss-Prot : SWS_FT_FI5

28) chain A
residue 230-251
type prosite
sequence SFDVDGLDPVFTPATGTPVVGG
description ARGINASE_1 Arginase family signature. SFDVDgldPvftPAtgtpvvgG
source prosite : PS01053


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