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4IW3

Crystal structure of a Pseudomonas putida prolyl-4-hydroxylase (P4H) in complex with elongation factor Tu (EF-Tu)

Functional Information from GO Data
ChainGOidnamespacecontents
A0005506molecular_functioniron ion binding
A0005737cellular_componentcytoplasm
A0008198molecular_functionferrous iron binding
A0016491molecular_functionoxidoreductase activity
A0016705molecular_functionoxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
A0031418molecular_functionL-ascorbic acid binding
A0031545molecular_functionpeptidyl-proline 4-dioxygenase activity
A0046872molecular_functionmetal ion binding
A0051213molecular_functiondioxygenase activity
A0071456biological_processcellular response to hypoxia
B0000166molecular_functionnucleotide binding
B0003746molecular_functiontranslation elongation factor activity
B0003924molecular_functionGTPase activity
B0005525molecular_functionGTP binding
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0006412biological_processtranslation
B0006414biological_processtranslational elongation
B0097216molecular_functionguanosine tetraphosphate binding
J0005506molecular_functioniron ion binding
J0005737cellular_componentcytoplasm
J0008198molecular_functionferrous iron binding
J0016491molecular_functionoxidoreductase activity
J0016705molecular_functionoxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
J0031418molecular_functionL-ascorbic acid binding
J0031545molecular_functionpeptidyl-proline 4-dioxygenase activity
J0046872molecular_functionmetal ion binding
J0051213molecular_functiondioxygenase activity
J0071456biological_processcellular response to hypoxia
K0000166molecular_functionnucleotide binding
K0003746molecular_functiontranslation elongation factor activity
K0003924molecular_functionGTPase activity
K0005525molecular_functionGTP binding
K0005737cellular_componentcytoplasm
K0005829cellular_componentcytosol
K0006412biological_processtranslation
K0006414biological_processtranslational elongation
K0097216molecular_functionguanosine tetraphosphate binding
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MN A 401
ChainResidue
AHIS124
AASP126
AHIS183
AOGA402
AHOH563

site_idAC2
Number of Residues14
DetailsBINDING SITE FOR RESIDUE OGA A 402
ChainResidue
AHIS183
AVAL185
AARG192
ATHR196
ATRP198
AMN401
AHOH504
AHOH540
AHOH563
BPRO54
AHIS124
AASP126
ATYR141
ALEU154

site_idAC3
Number of Residues16
DetailsBINDING SITE FOR RESIDUE GDP B 501
ChainResidue
BHIS20
BASP22
BHIS23
BGLY24
BLYS25
BTHR26
BTHR27
BASN136
BLYS137
BASP139
BSER174
BALA175
BARG176
BARG176
BMG502
BHOH616

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG B 502
ChainResidue
BLYS25
BTHR26
BCYS82
BGDP501
BHOH616

site_idAC5
Number of Residues7
DetailsBINDING SITE FOR RESIDUE MG K 401
ChainResidue
KTHR26
KASP81
KCYS82
KGDP402
KHOH525
KHOH536
KHOH537

site_idAC6
Number of Residues19
DetailsBINDING SITE FOR RESIDUE GDP K 402
ChainResidue
KHIS20
KVAL21
KASP22
KHIS23
KGLY24
KLYS25
KTHR26
KTHR27
KASN136
KLYS137
KASP139
KLEU140
KSER174
KALA175
KARG176
KARG176
KMG401
KHOH525
KHOH537

site_idAC7
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MN J 401
ChainResidue
JHIS124
JASP126
JHIS183
JOGA402
JHOH532

site_idAC8
Number of Residues16
DetailsBINDING SITE FOR RESIDUE OGA J 402
ChainResidue
JTYR121
JHIS124
JASP126
JVAL139
JTYR141
JLEU154
JHIS183
JVAL185
JARG192
JTHR196
JTRP198
JMN401
JHOH524
JHOH532
JHOH533
KPRO54

Functional Information from PROSITE/UniProt
site_idPS00301
Number of Residues16
DetailsG_TR_1 Translational (tr)-type guanine nucleotide-binding (G) domain signature. DSapeEKaRGITIntA
ChainResidueDetails
BASP51-ALA66

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues6
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00118
ChainResidueDetails
BGLY19
BASP81
BASN136
KGLY19
KASP81
KASN136

218853

PDB entries from 2024-04-24

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