|
eF-site ID
|
1amp-A |
PDB Code
|
1amp |
Chain
|
A |
|
click to enlarge
|
|
Title
|
CRYSTAL STRUCTURE OF AEROMONAS PROTEOLYTICA AMINOPEPTIDASE: A PROTOTYPICAL MEMBER OF THE CO-CATALYTIC ZINC ENZYME FAMILY |
Classification
|
HYDROLASE(AMINOPEPTIDASE) |
Compound
|
AMINOPEPTIDASE |
Source
|
Vibrio proteolyticus (Aeromonas proteolytica) (AMPX_VIBPR) |
|
Sequence
|
A: |
MPPITQQATVTAWLPQVDASQITGTISSLESFTNRFYTTT
SGAQASDWIASEWQALSASLPNASVKQVSHSGYNQKSVVM
TITGSEAPDEWIVIGGHLDSTIGSHTNEQSVAPGADDDAS
GIAAVTEVIRVLSENNFQPKRSIAFMAYAAEEVGLRGSQD
LANQYKSEGKNVVSALQLDMTNYKGSAQDVVFITDYTDSN
FTQYLTQLMDEYLPSLTYGFDTCGYACSDHASWHNAGYPA
AMPFESKFNDYNPRIHTTQDTLANSDPTGSHAKKFTQLGL
AYAIEMGSATG
|
|
Description
|
|
Functional site
|
|
1)
|
chain |
A |
residue |
117 |
type |
|
sequence |
D
|
description |
BINDING SITE FOR RESIDUE ZN A 501
|
source |
: AC1
|
|
2)
|
chain |
A |
residue |
152 |
type |
|
sequence |
E
|
description |
BINDING SITE FOR RESIDUE ZN A 501
|
source |
: AC1
|
|
3)
|
chain |
A |
residue |
256 |
type |
|
sequence |
H
|
description |
BINDING SITE FOR RESIDUE ZN A 501
|
source |
: AC1
|
|
4)
|
chain |
A |
residue |
97 |
type |
|
sequence |
H
|
description |
BINDING SITE FOR RESIDUE ZN A 502
|
source |
: AC2
|
|
5)
|
chain |
A |
residue |
117 |
type |
|
sequence |
D
|
description |
BINDING SITE FOR RESIDUE ZN A 502
|
source |
: AC2
|
|
6)
|
chain |
A |
residue |
179 |
type |
|
sequence |
D
|
description |
BINDING SITE FOR RESIDUE ZN A 502
|
source |
: AC2
|
|
7)
|
chain |
A |
residue |
97 |
type |
catalytic |
sequence |
H
|
description |
167
|
source |
MCSA : MCSA1
|
|
8)
|
chain |
A |
residue |
117 |
type |
catalytic |
sequence |
D
|
description |
167
|
source |
MCSA : MCSA1
|
|
9)
|
chain |
A |
residue |
151 |
type |
catalytic |
sequence |
E
|
description |
167
|
source |
MCSA : MCSA1
|
|
10)
|
chain |
A |
residue |
152 |
type |
catalytic |
sequence |
E
|
description |
167
|
source |
MCSA : MCSA1
|
|
11)
|
chain |
A |
residue |
179 |
type |
catalytic |
sequence |
D
|
description |
167
|
source |
MCSA : MCSA1
|
|
12)
|
chain |
A |
residue |
256 |
type |
catalytic |
sequence |
H
|
description |
167
|
source |
MCSA : MCSA1
|
|
13)
|
chain |
A |
residue |
97 |
type |
BINDING |
sequence |
H
|
description |
BINDING => ECO:0000269|PubMed:10413478, ECO:0000269|PubMed:11401547, ECO:0000269|PubMed:8087555, ECO:0000269|PubMed:8647077, ECO:0007744|PDB:1AMP, ECO:0007744|PDB:1CP6, ECO:0007744|PDB:1FT7, ECO:0007744|PDB:1IGB, ECO:0007744|PDB:1LOK, ECO:0007744|PDB:1RTQ, ECO:0007744|PDB:1TXR, ECO:0007744|PDB:1XRY, ECO:0007744|PDB:2ANP, ECO:0007744|PDB:2DEA, ECO:0007744|PDB:2IQ6, ECO:0007744|PDB:2NYQ, ECO:0007744|PDB:3B35, ECO:0007744|PDB:3B3C, ECO:0007744|PDB:3B3S, ECO:0007744|PDB:3B3T, ECO:0007744|PDB:3B3V, ECO:0007744|PDB:3B3W, ECO:0007744|PDB:3B7I, ECO:0007744|PDB:3FH4, ECO:0007744|PDB:3VH9
|
source |
Swiss-Prot : SWS_FT_FI1
|
|
14)
|
chain |
A |
residue |
117 |
type |
BINDING |
sequence |
D
|
description |
BINDING => ECO:0000269|PubMed:10413478, ECO:0000269|PubMed:11401547, ECO:0000269|PubMed:8087555, ECO:0000269|PubMed:8647077, ECO:0007744|PDB:1AMP, ECO:0007744|PDB:1CP6, ECO:0007744|PDB:1FT7, ECO:0007744|PDB:1IGB, ECO:0007744|PDB:1LOK, ECO:0007744|PDB:1RTQ, ECO:0007744|PDB:1TXR, ECO:0007744|PDB:1XRY, ECO:0007744|PDB:2ANP, ECO:0007744|PDB:2DEA, ECO:0007744|PDB:2IQ6, ECO:0007744|PDB:2NYQ, ECO:0007744|PDB:3B35, ECO:0007744|PDB:3B3C, ECO:0007744|PDB:3B3S, ECO:0007744|PDB:3B3T, ECO:0007744|PDB:3B3V, ECO:0007744|PDB:3B3W, ECO:0007744|PDB:3B7I, ECO:0007744|PDB:3FH4, ECO:0007744|PDB:3VH9
|
source |
Swiss-Prot : SWS_FT_FI1
|
|
15)
|
chain |
A |
residue |
152 |
type |
BINDING |
sequence |
E
|
description |
BINDING => ECO:0000269|PubMed:10413478, ECO:0000269|PubMed:11401547, ECO:0000269|PubMed:8087555, ECO:0000269|PubMed:8647077, ECO:0007744|PDB:1AMP, ECO:0007744|PDB:1CP6, ECO:0007744|PDB:1FT7, ECO:0007744|PDB:1IGB, ECO:0007744|PDB:1LOK, ECO:0007744|PDB:1RTQ, ECO:0007744|PDB:1TXR, ECO:0007744|PDB:1XRY, ECO:0007744|PDB:2ANP, ECO:0007744|PDB:2DEA, ECO:0007744|PDB:2IQ6, ECO:0007744|PDB:2NYQ, ECO:0007744|PDB:3B35, ECO:0007744|PDB:3B3C, ECO:0007744|PDB:3B3S, ECO:0007744|PDB:3B3T, ECO:0007744|PDB:3B3V, ECO:0007744|PDB:3B3W, ECO:0007744|PDB:3B7I, ECO:0007744|PDB:3FH4, ECO:0007744|PDB:3VH9
|
source |
Swiss-Prot : SWS_FT_FI1
|
|
16)
|
chain |
A |
residue |
179 |
type |
BINDING |
sequence |
D
|
description |
BINDING => ECO:0000269|PubMed:10413478, ECO:0000269|PubMed:11401547, ECO:0000269|PubMed:8087555, ECO:0000269|PubMed:8647077, ECO:0007744|PDB:1AMP, ECO:0007744|PDB:1CP6, ECO:0007744|PDB:1FT7, ECO:0007744|PDB:1IGB, ECO:0007744|PDB:1LOK, ECO:0007744|PDB:1RTQ, ECO:0007744|PDB:1TXR, ECO:0007744|PDB:1XRY, ECO:0007744|PDB:2ANP, ECO:0007744|PDB:2DEA, ECO:0007744|PDB:2IQ6, ECO:0007744|PDB:2NYQ, ECO:0007744|PDB:3B35, ECO:0007744|PDB:3B3C, ECO:0007744|PDB:3B3S, ECO:0007744|PDB:3B3T, ECO:0007744|PDB:3B3V, ECO:0007744|PDB:3B3W, ECO:0007744|PDB:3B7I, ECO:0007744|PDB:3FH4, ECO:0007744|PDB:3VH9
|
source |
Swiss-Prot : SWS_FT_FI1
|
|
17)
|
chain |
A |
residue |
256 |
type |
BINDING |
sequence |
H
|
description |
BINDING => ECO:0000269|PubMed:10413478, ECO:0000269|PubMed:11401547, ECO:0000269|PubMed:8087555, ECO:0000269|PubMed:8647077, ECO:0007744|PDB:1AMP, ECO:0007744|PDB:1CP6, ECO:0007744|PDB:1FT7, ECO:0007744|PDB:1IGB, ECO:0007744|PDB:1LOK, ECO:0007744|PDB:1RTQ, ECO:0007744|PDB:1TXR, ECO:0007744|PDB:1XRY, ECO:0007744|PDB:2ANP, ECO:0007744|PDB:2DEA, ECO:0007744|PDB:2IQ6, ECO:0007744|PDB:2NYQ, ECO:0007744|PDB:3B35, ECO:0007744|PDB:3B3C, ECO:0007744|PDB:3B3S, ECO:0007744|PDB:3B3T, ECO:0007744|PDB:3B3V, ECO:0007744|PDB:3B3W, ECO:0007744|PDB:3B7I, ECO:0007744|PDB:3FH4, ECO:0007744|PDB:3VH9
|
source |
Swiss-Prot : SWS_FT_FI1
|
|
|
|