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1U5U

The structure of an Allene Oxide Synthase reveals a novel use for a catalase fold

Functional Information from GO Data
ChainGOidnamespacecontents
A0020037molecular_functionheme binding
B0020037molecular_functionheme binding
Functional Information from PDB Data
site_idAC1
Number of Residues25
DetailsBINDING SITE FOR RESIDUE HEM A 999
ChainResidue
APHE53
AASN137
AASN142
APHE144
AGLN195
AVAL196
APHE322
AARG349
AVAL352
ATYR353
AGLN357
AARG64
AARG360
AHOH1001
AHOH1002
AHOH1014
AHOH1059
AHOH1122
ATHR66
AHIS67
AARG102
ASER118
ASER120
AVAL135
AMET136

site_idAC2
Number of Residues25
DetailsBINDING SITE FOR RESIDUE HEM B 999
ChainResidue
BPHE53
BARG64
BTHR66
BHIS67
BARG102
BSER118
BSER120
BVAL135
BMET136
BASN137
BASN142
BPHE144
BGLN195
BVAL196
BPHE322
BARG349
BVAL352
BTYR353
BVAL356
BGLN357
BARG360
BHOH1004
BHOH1011
BHOH1018
BHOH1087

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsBINDING: axial binding residue
ChainResidueDetails
ATYR353
BTYR353

Catalytic Information from CSA
site_idCSA1
Number of Residues4
Detailsa catalytic site defined by CSA, PubMed 15625113, 12779342, 16513636
ChainResidueDetails
ATYR193
AASN137
ATHR66
AHIS67

site_idCSA2
Number of Residues4
Detailsa catalytic site defined by CSA, PubMed 15625113, 12779342, 16513636
ChainResidueDetails
BTYR193
BASN137
BTHR66
BHIS67

site_idMCSA1
Number of Residues4
DetailsM-CSA 758
ChainResidueDetails
ATHR66electrostatic stabiliser
AHIS67electrostatic stabiliser, proton acceptor, proton donor
AASN137electrostatic stabiliser
ATYR353metal ligand

site_idMCSA2
Number of Residues4
DetailsM-CSA 758
ChainResidueDetails
BTHR66electrostatic stabiliser
BHIS67electrostatic stabiliser, proton acceptor, proton donor
BASN137electrostatic stabiliser
BTYR353metal ligand

226707

PDB entries from 2024-10-30

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