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eF-site ID
|
1amp-A |
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PDB Code
|
1amp |
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Chain
|
A |
|
click to enlarge
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Title
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CRYSTAL STRUCTURE OF AEROMONAS PROTEOLYTICA AMINOPEPTIDASE: A PROTOTYPICAL MEMBER OF THE CO-CATALYTIC ZINC ENZYME FAMILY |
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Classification
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HYDROLASE(AMINOPEPTIDASE) |
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Compound
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AMINOPEPTIDASE |
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Source
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Vibrio proteolyticus (Aeromonas proteolytica) (AMPX_VIBPR) |
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Sequence
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A: |
MPPITQQATVTAWLPQVDASQITGTISSLESFTNRFYTTT
SGAQASDWIASEWQALSASLPNASVKQVSHSGYNQKSVVM
TITGSEAPDEWIVIGGHLDSTIGSHTNEQSVAPGADDDAS
GIAAVTEVIRVLSENNFQPKRSIAFMAYAAEEVGLRGSQD
LANQYKSEGKNVVSALQLDMTNYKGSAQDVVFITDYTDSN
FTQYLTQLMDEYLPSLTYGFDTCGYACSDHASWHNAGYPA
AMPFESKFNDYNPRIHTTQDTLANSDPTGSHAKKFTQLGL
AYAIEMGSATG
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Description
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Functional site
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|
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1)
|
chain |
A |
| residue |
117 |
| type |
|
| sequence |
D
|
| description |
BINDING SITE FOR RESIDUE ZN A 501
|
| source |
: AC1
|
|
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2)
|
chain |
A |
| residue |
152 |
| type |
|
| sequence |
E
|
| description |
BINDING SITE FOR RESIDUE ZN A 501
|
| source |
: AC1
|
|
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3)
|
chain |
A |
| residue |
256 |
| type |
|
| sequence |
H
|
| description |
BINDING SITE FOR RESIDUE ZN A 501
|
| source |
: AC1
|
|
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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
|
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