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3FVZ

Structure of Peptidyl-alpha-hydroxyglycine alpha-Amidating Lyase (PAL)

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0006518biological_processpeptide metabolic process
A0016020cellular_componentmembrane
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN A 821
ChainResidue
AACT1
AHIS585
ATYR654
AHIS690
AHIS786

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE FE A 822
ChainResidue
AHIS492
AHIS493
AASP498
AILE572

site_idAC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE CA A 823
ChainResidue
AHOH25
AHOH54
AHOH56
AVAL520
ALEU587
AASP787
AGOL824

site_idAC4
Number of Residues9
DetailsBINDING SITE FOR RESIDUE ACT A 1
ChainResidue
AHOH75
AARG533
ATRP538
AHIS585
ATYR654
AHIS690
AMET784
AHIS786
AZN821

site_idAC5
Number of Residues8
DetailsBINDING SITE FOR RESIDUE GOL A 824
ChainResidue
ASER518
AGLY586
ALEU587
AASP638
AHIS690
AHIS786
AASP787
ACA823

site_idAC6
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL A 2
ChainResidue
AHOH74
AHOH112
AVAL778
AARG779
ALYS780
AGLU792
AASP793

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsBINDING: BINDING => ECO:0000269|PubMed:19604476, ECO:0007744|PDB:3FVZ, ECO:0007744|PDB:3FW0
ChainResidueDetails
AVAL520
ALEU587
AASP787

site_idSWS_FT_FI2
Number of Residues3
DetailsBINDING: BINDING => ECO:0000305|PubMed:19604476, ECO:0007744|PDB:3FW0
ChainResidueDetails
AARG533
ATYR654
AARG706

site_idSWS_FT_FI3
Number of Residues3
DetailsBINDING: BINDING => ECO:0000269|PubMed:19604476, ECO:0007744|PDB:3FVZ
ChainResidueDetails
AHIS585
AHIS690
AHIS786

site_idSWS_FT_FI4
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:2211657
ChainResidueDetails
AASN765

Catalytic Information from CSA
site_idMCSA1
Number of Residues
DetailsM-CSA 135
ChainResidueDetails

222926

PDB entries from 2024-07-24

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