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1M70

Crystal structure of oxidized recombinant cytochrome c4 from Pseudomonas stutzeri

Functional Information from GO Data
ChainGOidnamespacecontents
A0005506molecular_functioniron ion binding
A0009055molecular_functionelectron transfer activity
A0020037molecular_functionheme binding
A0042597cellular_componentperiplasmic space
A0046872molecular_functionmetal ion binding
B0005506molecular_functioniron ion binding
B0009055molecular_functionelectron transfer activity
B0020037molecular_functionheme binding
B0042597cellular_componentperiplasmic space
B0046872molecular_functionmetal ion binding
C0005506molecular_functioniron ion binding
C0009055molecular_functionelectron transfer activity
C0020037molecular_functionheme binding
C0042597cellular_componentperiplasmic space
C0046872molecular_functionmetal ion binding
D0005506molecular_functioniron ion binding
D0009055molecular_functionelectron transfer activity
D0020037molecular_functionheme binding
D0042597cellular_componentperiplasmic space
D0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues24
DetailsBINDING SITE FOR RESIDUE HEC A 199
ChainResidue
AVAL13
AILE47
AARG61
AVAL63
AGLU65
AMET66
AMET69
ALEU70
AILE81
ATYR145
ALYS148
ACYS14
AGLN149
AHEC200
AHOH204
AHOH232
AHOH316
ACYS17
AHIS18
APHE29
APRO30
ALEU32
ATYR39
AGLN43

site_idAC2
Number of Residues19
DetailsBINDING SITE FOR RESIDUE HEC A 200
ChainResidue
ATYR39
ALYS42
AGLN43
AALA118
ACYS119
ACYS122
AHIS123
APRO136
ALEU138
ATYR145
AGLN149
AARG158
AASN160
AILE166
AMET167
AHEC199
AHOH202
AHOH272
AHOH341

site_idAC3
Number of Residues21
DetailsBINDING SITE FOR RESIDUE HEC B 199
ChainResidue
BVAL13
BCYS14
BCYS17
BHIS18
BPHE29
BPRO30
BTYR39
BGLN43
BILE47
BARG61
BVAL63
BGLU65
BMET66
BMET69
BLEU70
BTYR145
BLYS148
BGLN149
BHEC200
BHOH203
BHOH219

site_idAC4
Number of Residues19
DetailsBINDING SITE FOR RESIDUE HEC B 200
ChainResidue
BTYR39
BLYS42
BGLN43
BALA118
BCYS119
BCYS122
BHIS123
BPHE135
BPRO136
BLEU138
BTYR145
BARG158
BASN160
BILE166
BMET167
BHEC199
BHOH201
BHOH340
DALA16

site_idAC5
Number of Residues23
DetailsBINDING SITE FOR RESIDUE HEC C 199
ChainResidue
CILE81
CTYR145
CLYS148
CGLN149
CHEC200
CHOH201
CHOH273
APHE135
CVAL13
CCYS14
CCYS17
CHIS18
CPHE29
CTYR39
CGLN43
CLEU44
CILE47
CARG61
CVAL63
CGLU65
CMET66
CMET69
CLEU70

site_idAC6
Number of Residues20
DetailsBINDING SITE FOR RESIDUE HEC C 200
ChainResidue
BALA16
CTYR39
CLYS42
CGLN43
CALA118
CCYS119
CCYS122
CHIS123
CPHE135
CPRO136
CLEU138
CTYR145
CARG158
CASN160
CMET167
CVAL170
CHEC199
CHOH204
CHOH219
CHOH223

site_idAC7
Number of Residues25
DetailsBINDING SITE FOR RESIDUE HEC D 199
ChainResidue
BPHE135
DVAL13
DCYS14
DCYS17
DHIS18
DPHE29
DPRO30
DTYR39
DGLN43
DLEU44
DILE47
DARG61
DVAL63
DGLU65
DMET66
DMET69
DLEU70
DILE81
DTYR145
DLYS148
DGLN149
DHEC200
DHOH201
DHOH243
DHOH294

site_idAC8
Number of Residues22
DetailsBINDING SITE FOR RESIDUE HEC D 200
ChainResidue
AALA16
DTYR39
DLYS42
DGLN43
DALA118
DCYS119
DCYS122
DHIS123
DPHE135
DPRO136
DLEU138
DTYR145
DGLN149
DARG158
DASN160
DILE166
DMET167
DVAL170
DHEC199
DHOH202
DHOH225
DHOH247

site_idAC9
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL A 201
ChainResidue
AGLY188
ALEU189
AHIS190
AHOH205
AHOH225

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues16
DetailsBINDING: covalent
ChainResidueDetails
ACYS14
CCYS17
CCYS119
CCYS122
DCYS14
DCYS17
DCYS119
DCYS122
ACYS17
ACYS119
ACYS122
BCYS14
BCYS17
BCYS119
BCYS122
CCYS14

site_idSWS_FT_FI2
Number of Residues16
DetailsBINDING: axial binding residue
ChainResidueDetails
AHIS18
CMET66
CHIS123
CMET167
DHIS18
DMET66
DHIS123
DMET167
AMET66
AHIS123
AMET167
BHIS18
BMET66
BHIS123
BMET167
CHIS18

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PDB entries from 2024-04-24

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