|
|
1)
|
chain |
A |
residue |
195 |
type |
|
sequence |
D
|
description |
DIRECT METAL ION LIGANDS
|
source |
: MTL
|
|
2)
|
chain |
A |
residue |
221 |
type |
|
sequence |
E
|
description |
DIRECT METAL ION LIGANDS
|
source |
: MTL
|
|
3)
|
chain |
A |
residue |
247 |
type |
|
sequence |
E
|
description |
DIRECT METAL ION LIGANDS
|
source |
: MTL
|
|
4)
|
chain |
A |
residue |
166 |
type |
|
sequence |
K
|
description |
ACID/BASE CATALYSTS RESPONSIBLE FOR PROTON ABSTRACTION AND REDELIVERY IN THE RACEMIZATION REACTION
|
source |
: ACT
|
|
5)
|
chain |
A |
residue |
297 |
type |
|
sequence |
H
|
description |
ACID/BASE CATALYSTS RESPONSIBLE FOR PROTON ABSTRACTION AND REDELIVERY IN THE RACEMIZATION REACTION
|
source |
: ACT
|
|
6)
|
chain |
A |
residue |
164 |
type |
|
sequence |
K
|
description |
BINDING SITE FOR THE CARBOXYL GROUP OF SUBSTRATE. THESE RESIDUES FUNCTION, ALONG WITH THE METAL ION, AS ELECTROPHILIC CATALYSTS
|
source |
: CAR
|
|
7)
|
chain |
A |
residue |
317 |
type |
|
sequence |
E
|
description |
BINDING SITE FOR THE CARBOXYL GROUP OF SUBSTRATE. THESE RESIDUES FUNCTION, ALONG WITH THE METAL ION, AS ELECTROPHILIC CATALYSTS
|
source |
: CAR
|
|
8)
|
chain |
A |
residue |
195 |
type |
|
sequence |
D
|
description |
BINDING SITE FOR RESIDUE MG A 360
|
source |
: AC1
|
|
9)
|
chain |
A |
residue |
221 |
type |
|
sequence |
E
|
description |
BINDING SITE FOR RESIDUE MG A 360
|
source |
: AC1
|
|
10)
|
chain |
A |
residue |
247 |
type |
|
sequence |
E
|
description |
BINDING SITE FOR RESIDUE MG A 360
|
source |
: AC1
|
|
11)
|
chain |
A |
residue |
164 |
type |
|
sequence |
K
|
description |
BINDING SITE FOR RESIDUE APG A 399
|
source |
: AC2
|
|
12)
|
chain |
A |
residue |
166 |
type |
|
sequence |
K
|
description |
BINDING SITE FOR RESIDUE APG A 399
|
source |
: AC2
|
|
13)
|
chain |
A |
residue |
195 |
type |
|
sequence |
D
|
description |
BINDING SITE FOR RESIDUE APG A 399
|
source |
: AC2
|
|
14)
|
chain |
A |
residue |
197 |
type |
|
sequence |
N
|
description |
BINDING SITE FOR RESIDUE APG A 399
|
source |
: AC2
|
|
15)
|
chain |
A |
residue |
221 |
type |
|
sequence |
E
|
description |
BINDING SITE FOR RESIDUE APG A 399
|
source |
: AC2
|
|
16)
|
chain |
A |
residue |
247 |
type |
|
sequence |
E
|
description |
BINDING SITE FOR RESIDUE APG A 399
|
source |
: AC2
|
|
17)
|
chain |
A |
residue |
297 |
type |
|
sequence |
H
|
description |
BINDING SITE FOR RESIDUE APG A 399
|
source |
: AC2
|
|
18)
|
chain |
A |
residue |
317 |
type |
|
sequence |
E
|
description |
BINDING SITE FOR RESIDUE APG A 399
|
source |
: AC2
|
|
19)
|
chain |
A |
residue |
164 |
type |
catalytic |
sequence |
K
|
description |
187
|
source |
MCSA : MCSA1
|
|
20)
|
chain |
A |
residue |
166 |
type |
catalytic |
sequence |
K
|
description |
187
|
source |
MCSA : MCSA1
|
|
21)
|
chain |
A |
residue |
195 |
type |
catalytic |
sequence |
D
|
description |
187
|
source |
MCSA : MCSA1
|
|
22)
|
chain |
A |
residue |
197 |
type |
catalytic |
sequence |
N
|
description |
187
|
source |
MCSA : MCSA1
|
|
23)
|
chain |
A |
residue |
221 |
type |
catalytic |
sequence |
E
|
description |
187
|
source |
MCSA : MCSA1
|
|
24)
|
chain |
A |
residue |
247 |
type |
catalytic |
sequence |
E
|
description |
187
|
source |
MCSA : MCSA1
|
|
25)
|
chain |
A |
residue |
270 |
type |
catalytic |
sequence |
D
|
description |
187
|
source |
MCSA : MCSA1
|
|
26)
|
chain |
A |
residue |
297 |
type |
catalytic |
sequence |
H
|
description |
187
|
source |
MCSA : MCSA1
|
|
27)
|
chain |
A |
residue |
317 |
type |
catalytic |
sequence |
E
|
description |
187
|
source |
MCSA : MCSA1
|
|
28)
|
chain |
A |
residue |
103-128 |
type |
prosite |
sequence |
AAAGIDMAAWDALGKVHETPLVKLLG
|
description |
MR_MLE_1 Mandelate racemase / muconate lactonizing enzyme family signature 1. AaAGIDmAAwDAlGKvhetPLvkLLG
|
source |
prosite : PS00908
|
|
29)
|
chain |
A |
residue |
192-223 |
type |
prosite |
sequence |
IMVDYNQSLDVPAAIKRSQALQQEGVTWIEEP
|
description |
MR_MLE_2 Mandelate racemase / muconate lactonizing enzyme family signature 2. ImvDyNqsldvpaAikrsqaLqqegvtwIEEP
|
source |
prosite : PS00909
|
|
30)
|
chain |
A |
residue |
166 |
type |
ACT_SITE |
sequence |
K
|
description |
Proton acceptor; specific for S-mandelate
|
source |
Swiss-Prot : SWS_FT_FI1
|
|
31)
|
chain |
A |
residue |
297 |
type |
ACT_SITE |
sequence |
H
|
description |
Proton acceptor; specific for R-mandelate
|
source |
Swiss-Prot : SWS_FT_FI2
|
|
32)
|
chain |
A |
residue |
195 |
type |
BINDING |
sequence |
D
|
description |
BINDING => ECO:0000269|PubMed:7893689, ECO:0000269|PubMed:7893690, ECO:0000305|PubMed:1892834
|
source |
Swiss-Prot : SWS_FT_FI3
|
|
33)
|
chain |
A |
residue |
221 |
type |
BINDING |
sequence |
E
|
description |
BINDING => ECO:0000269|PubMed:7893689, ECO:0000269|PubMed:7893690, ECO:0000305|PubMed:1892834
|
source |
Swiss-Prot : SWS_FT_FI3
|
|
34)
|
chain |
A |
residue |
247 |
type |
BINDING |
sequence |
E
|
description |
BINDING => ECO:0000269|PubMed:7893689, ECO:0000269|PubMed:7893690, ECO:0000305|PubMed:1892834
|
source |
Swiss-Prot : SWS_FT_FI3
|
|
35)
|
chain |
A |
residue |
317 |
type |
BINDING |
sequence |
E
|
description |
BINDING => ECO:0000269|PubMed:7893689, ECO:0000269|PubMed:7893690, ECO:0000305|PubMed:1892834
|
source |
Swiss-Prot : SWS_FT_FI3
|
|