eF-site ID 6i0k-A
PDB Code 6i0k
Chain A

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Title Structure of quinolinate synthase in complex with 4-mercaptophthalic acid
Classification TRANSFERASE
Compound Quinolinate synthase A
Source (NADA_THEMA)
Sequence A:  HHHMVDEILKLKKEKGYIILAHNFQIPELQDIADFVGDSL
QLARKAMELSEKKILFLGVDFMAELVKILNPDKKVIVPDR
SATCPMANRLTPEIIREYREKFPDAPVVLYVNSTSECKTL
ADVICTSANAVEVVKKLDSSVVIFGPDRNLGEYVAEKTGK
KVITIPENGHCPVHQFNAESIDAVRKKYPDAKVIVHPECP
KPVRDKADYVGSTGQMEKIPERDPSRIFVIGTEIGMIHKL
KKKFPDREFVPLEMAVCVNMKKNTLENTLHALQTESFEVI
LPKEVIEKAKKPILRMFELMG
Description


Functional site
1) chain A
residue 81
type
sequence C
description binding site for residue SF4 A 301
source : AC1
2) chain A
residue 109
type
sequence N
description binding site for residue SF4 A 301
source : AC1
3) chain A
residue 168
type
sequence C
description binding site for residue SF4 A 301
source : AC1
4) chain A
residue 254
type
sequence C
description binding site for residue SF4 A 301
source : AC1
5) chain A
residue 19
type
sequence H
description binding site for residue GZ8 A 302
source : AC2
6) chain A
residue 21
type
sequence F
description binding site for residue GZ8 A 302
source : AC2
7) chain A
residue 35
type
sequence D
description binding site for residue GZ8 A 302
source : AC2
8) chain A
residue 36
type
sequence S
description binding site for residue GZ8 A 302
source : AC2
9) chain A
residue 59
type
sequence M
description binding site for residue GZ8 A 302
source : AC2
10) chain A
residue 109
type
sequence N
description binding site for residue GZ8 A 302
source : AC2
11) chain A
residue 124
type
sequence S
description binding site for residue GZ8 A 302
source : AC2
12) chain A
residue 193
type
sequence H
description binding site for residue GZ8 A 302
source : AC2
13) chain A
residue 209
type
sequence S
description binding site for residue GZ8 A 302
source : AC2
14) chain A
residue 210
type
sequence T
description binding site for residue GZ8 A 302
source : AC2
15) chain A
residue -1
type
sequence H
description binding site for residue PO4 A 303
source : AC3
16) chain A
residue 0
type
sequence H
description binding site for residue PO4 A 303
source : AC3
17) chain A
residue 1
type
sequence M
description binding site for residue PO4 A 303
source : AC3
18) chain A
residue 2
type
sequence V
description binding site for residue PO4 A 303
source : AC3
19) chain A
residue 67
type
sequence N
description binding site for residue CL A 304
source : AC4
20) chain A
residue 69
type
sequence D
description binding site for residue CL A 304
source : AC4
21) chain A
residue 193
type BINDING
sequence H
description BINDING => ECO:0000255|HAMAP-Rule:MF_00568, ECO:0000305|PubMed:27545412, ECO:0000305|PubMed:29641168, ECO:0000305|PubMed:30855610
source Swiss-Prot : SWS_FT_FI1
22) chain A
residue 210
type BINDING
sequence T
description BINDING => ECO:0000255|HAMAP-Rule:MF_00568, ECO:0000305|PubMed:27545412, ECO:0000305|PubMed:29641168, ECO:0000305|PubMed:30855610
source Swiss-Prot : SWS_FT_FI1
23) chain A
residue 19
type BINDING
sequence H
description BINDING => ECO:0000255|HAMAP-Rule:MF_00568, ECO:0000305|PubMed:27545412, ECO:0000305|PubMed:29641168, ECO:0000305|PubMed:30855610
source Swiss-Prot : SWS_FT_FI1
24) chain A
residue 36
type BINDING
sequence S
description BINDING => ECO:0000255|HAMAP-Rule:MF_00568, ECO:0000305|PubMed:27545412, ECO:0000305|PubMed:29641168, ECO:0000305|PubMed:30855610
source Swiss-Prot : SWS_FT_FI1
25) chain A
residue 124
type BINDING
sequence S
description BINDING => ECO:0000255|HAMAP-Rule:MF_00568, ECO:0000305|PubMed:27545412, ECO:0000305|PubMed:29641168, ECO:0000305|PubMed:30855610
source Swiss-Prot : SWS_FT_FI1
26) chain A
residue 168
type BINDING
sequence C
description BINDING => ECO:0000255|HAMAP-Rule:MF_00568, ECO:0000269|PubMed:24650327, ECO:0000269|PubMed:27545412, ECO:0000269|PubMed:29641168, ECO:0007744|PDB:4P3X, ECO:0007744|PDB:5F33, ECO:0007744|PDB:5F35, ECO:0007744|PDB:5F3D, ECO:0007744|PDB:5LQM, ECO:0007744|PDB:5LQS
source Swiss-Prot : SWS_FT_FI2
27) chain A
residue 254
type BINDING
sequence C
description BINDING => ECO:0000255|HAMAP-Rule:MF_00568, ECO:0000269|PubMed:24650327, ECO:0000269|PubMed:27545412, ECO:0000269|PubMed:29641168, ECO:0007744|PDB:4P3X, ECO:0007744|PDB:5F33, ECO:0007744|PDB:5F35, ECO:0007744|PDB:5F3D, ECO:0007744|PDB:5LQM, ECO:0007744|PDB:5LQS
source Swiss-Prot : SWS_FT_FI2
28) chain A
residue 81
type BINDING
sequence C
description BINDING => ECO:0000255|HAMAP-Rule:MF_00568, ECO:0000269|PubMed:24650327, ECO:0000269|PubMed:27545412, ECO:0000269|PubMed:29641168, ECO:0007744|PDB:4P3X, ECO:0007744|PDB:5F33, ECO:0007744|PDB:5F35, ECO:0007744|PDB:5F3D, ECO:0007744|PDB:5LQM, ECO:0007744|PDB:5LQS
source Swiss-Prot : SWS_FT_FI2
29) chain A
residue 107
type BINDING
sequence Y
description BINDING => ECO:0000255|HAMAP-Rule:MF_00568, ECO:0000305|PubMed:27545412, ECO:0000305|PubMed:29641168
source Swiss-Prot : SWS_FT_FI3

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