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3MDW

The structure of N-formimino-L-Glutamate Iminohydrolase from Pseudomonas aeruginosa complexed with N-formimino-L-Aspartate

Functional Information from GO Data
ChainGOidnamespacecontents
A0005829cellular_componentcytosol
A0006547biological_processL-histidine metabolic process
A0006548biological_processL-histidine catabolic process
A0016787molecular_functionhydrolase activity
A0016810molecular_functionhydrolase activity, acting on carbon-nitrogen (but not peptide) bonds
A0019239molecular_functiondeaminase activity
A0019556biological_processL-histidine catabolic process to glutamate and formamide
A0019557biological_processL-histidine catabolic process to glutamate and formate
A0046872molecular_functionmetal ion binding
A0050416molecular_functionformimidoylglutamate deiminase activity
B0005829cellular_componentcytosol
B0006547biological_processL-histidine metabolic process
B0006548biological_processL-histidine catabolic process
B0016787molecular_functionhydrolase activity
B0016810molecular_functionhydrolase activity, acting on carbon-nitrogen (but not peptide) bonds
B0019239molecular_functiondeaminase activity
B0019556biological_processL-histidine catabolic process to glutamate and formamide
B0019557biological_processL-histidine catabolic process to glutamate and formate
B0046872molecular_functionmetal ion binding
B0050416molecular_functionformimidoylglutamate deiminase activity
C0005829cellular_componentcytosol
C0006547biological_processL-histidine metabolic process
C0006548biological_processL-histidine catabolic process
C0016787molecular_functionhydrolase activity
C0016810molecular_functionhydrolase activity, acting on carbon-nitrogen (but not peptide) bonds
C0019239molecular_functiondeaminase activity
C0019556biological_processL-histidine catabolic process to glutamate and formamide
C0019557biological_processL-histidine catabolic process to glutamate and formate
C0046872molecular_functionmetal ion binding
C0050416molecular_functionformimidoylglutamate deiminase activity
D0005829cellular_componentcytosol
D0006547biological_processL-histidine metabolic process
D0006548biological_processL-histidine catabolic process
D0016787molecular_functionhydrolase activity
D0016810molecular_functionhydrolase activity, acting on carbon-nitrogen (but not peptide) bonds
D0019239molecular_functiondeaminase activity
D0019556biological_processL-histidine catabolic process to glutamate and formamide
D0019557biological_processL-histidine catabolic process to glutamate and formate
D0046872molecular_functionmetal ion binding
D0050416molecular_functionformimidoylglutamate deiminase activity
Functional Information from PDB Data
site_idAC1
Number of Residues15
DetailsBINDING SITE FOR RESIDUE NFQ A 454
ChainResidue
AHIS58
AASP320
AHOH505
AHOH508
AHOH539
AHOH568
AHOH1026
AGLN61
APHE78
AARG82
ATYR121
AHIS206
AARG209
AGLU235
ALEU298

site_idAC2
Number of Residues14
DetailsBINDING SITE FOR RESIDUE NFQ B 454
ChainResidue
BGLN61
BPHE78
BARG82
BTYR121
BHIS206
BARG209
BGLU235
BLEU298
BASP320
BHOH495
BHOH554
BHOH564
BHOH599
BHOH1021

site_idAC3
Number of Residues14
DetailsBINDING SITE FOR RESIDUE NFQ C 454
ChainResidue
CHIS58
CGLN61
CARG82
CTYR121
CHIS206
CARG209
CGLU235
CLEU298
CASP320
CHOH489
CHOH524
CHOH539
CHOH540
CHOH1024

site_idAC4
Number of Residues15
DetailsBINDING SITE FOR RESIDUE NFQ D 454
ChainResidue
DHIS58
DGLN61
DPHE78
DARG82
DTYR121
DHIS206
DARG209
DGLU235
DLEU298
DASP320
DHOH511
DHOH517
DHOH526
DHOH577
DHOH1023

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN A 455
ChainResidue
AHIS56
AHIS58
AHIS232
AASP320
AHOH1026

site_idAC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN B 455
ChainResidue
BHIS56
BHIS58
BHIS232
BASP320
BHOH1021

site_idAC7
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN C 455
ChainResidue
CHIS56
CHIS58
CHIS232
CASP320
CHOH1024

site_idAC8
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN D 455
ChainResidue
DHIS56
DHIS58
DHIS232
DASP320
DHOH1023

site_idAC9
Number of Residues9
DetailsBINDING SITE FOR RESIDUE GOL C 456
ChainResidue
AGLY179
AGLU181
AALA182
AHOH533
AHOH809
CHIS161
CTHR212
CGLN214
CGLN215

site_idBC1
Number of Residues8
DetailsBINDING SITE FOR RESIDUE GOL A 456
ChainResidue
ALEU11
APRO12
AARG358
AASP362
AGLY377
ASER378
AHOH469
AHOH483

site_idBC2
Number of Residues9
DetailsBINDING SITE FOR RESIDUE PO4 D 456
ChainResidue
DHIS161
DTHR212
DGLN214
DGLN215
DHOH798
BGLY179
BGLU181
BALA182
BHOH812

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues8
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"PubMed","id":"17128965","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"25559274","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues16
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"25559274","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3MDU","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3MDW","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4RDV","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4RDW","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4RZB","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues24
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"25559274","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"3MDU","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3MDW","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4RDV","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4RDW","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4RZB","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

246704

PDB entries from 2025-12-24

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