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3B3S

Crystal structure of the M180A mutant of the aminopeptidase from Vibrio proteolyticus in complex with leucine

Functional Information from GO Data
ChainGOidnamespacecontents
A0006508biological_processproteolysis
A0008235molecular_functionmetalloexopeptidase activity
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE ZN A 292
ChainResidue
AASP117
AGLU152
AHIS256
AZN293
ALEU304
AHOH412

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE ZN A 293
ChainResidue
AASP179
AZN292
ALEU304
AHOH412
AHIS97
AASP117
AGLU151

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE NA A 294
ChainResidue
ALEU213
APRO214
ASER215

site_idAC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE NA A 295
ChainResidue
AALA19
ALYS273
AHOH564

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE NA A 296
ChainResidue
AASP47
ATRP48
ASER51
AHOH502

site_idAC6
Number of Residues7
DetailsBINDING SITE FOR RESIDUE NA A 297
ChainResidue
ASER20
ATYR218
AHOH305
AHOH358
AHOH373
AHOH555
AHOH575

site_idAC7
Number of Residues5
DetailsBINDING SITE FOR RESIDUE NA A 298
ChainResidue
ATHR194
ATHR197
AHOH306
AHOH381
AHOH468

site_idAC8
Number of Residues1
DetailsBINDING SITE FOR RESIDUE NA A 299
ChainResidue
AHIS234

site_idAC9
Number of Residues1
DetailsBINDING SITE FOR RESIDUE NA A 300
ChainResidue
ANA301

site_idBC1
Number of Residues1
DetailsBINDING SITE FOR RESIDUE NA A 301
ChainResidue
ANA300

site_idBC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SCN A 302
ChainResidue
ATHR194
ASER199
ATHR202
AGLN203
ALEU262
AHOH306

site_idBC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SCN A 303
ChainResidue
AALA12
ATRP13
AHOH330

site_idBC4
Number of Residues13
DetailsBINDING SITE FOR RESIDUE LEU A 304
ChainResidue
AGLU151
AGLU152
AASP179
ATYR225
ACYS227
APHE248
AILE255
AHIS256
AZN292
AZN293
AHOH363
AHOH412
AHOH583

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues5
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"10413478","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"11401547","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8087555","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8647077","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1AMP","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1CP6","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1FT7","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1IGB","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1LOK","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1RTQ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1TXR","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1XRY","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2ANP","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2DEA","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2IQ6","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2NYQ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3B35","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3B3C","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3B3S","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3B3T","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3B3V","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3B3W","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3B7I","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3FH4","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3VH9","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues1
DetailsAnnotated By Reference To The Literature 1amp
ChainResidueDetails
AGLU151

site_idMCSA1
Number of Residues6
DetailsM-CSA 167
ChainResidueDetails
AHIS97metal ligand
AASP117metal ligand
AGLU151hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
AGLU152metal ligand
AASP179metal ligand
AHIS256metal ligand

239803

PDB entries from 2025-08-06

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