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6AY0

Crystal structure of H108A peptidylglycine alpha-hydroxylating monooxygenase (PHM) soaked with peptide

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0004497molecular_functionmonooxygenase activity
A0005507molecular_functioncopper ion binding
A0006518biological_processpeptide metabolic process
A0016020cellular_componentmembrane
A0016715molecular_functionoxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced ascorbate as one donor, and incorporation of one atom of oxygen
Functional Information from PDB Data
site_idAC1
Number of Residues3
Detailsbinding site for residue CU A 1001
ChainResidue
AHIS242
AHIS244
AMET314

Functional Information from PROSITE/UniProt
site_idPS00085
Number of Residues13
DetailsCU2_MONOOXYGENASE_2 Copper type II, ascorbate-dependent monooxygenases signature 2. HvFayrvHTHhlG
ChainResidueDetails
AHIS235-GLY247

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:10504734, ECO:0007744|PDB:1OPM, ECO:0007744|PDB:3PHM
ChainResidueDetails
AHIS107
AALA108
AHIS172
AHIS242
AHIS244
AMET314

Catalytic Information from CSA
site_idMCSA1
Number of Residues7
DetailsM-CSA 135
ChainResidueDetails
AHIS107metal ligand
AALA108hydrogen bond donor, metal ligand, single electron acceptor, single electron donor, single electron relay
AGLN170hydrogen bond acceptor, single electron acceptor, single electron donor, single electron relay
AHIS172metal ligand
AHIS242metal ligand
AHIS244metal ligand
AMET314metal ligand

224931

PDB entries from 2024-09-11

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