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6RTD

Dihydro-heme d1 dehydrogenase NirN in complex with DHE

Functional Information from GO Data
ChainGOidnamespacecontents
A0006783biological_processheme biosynthetic process
A0009055molecular_functionelectron transfer activity
A0016491molecular_functionoxidoreductase activity
A0020037molecular_functionheme binding
A0042597cellular_componentperiplasmic space
A0046872molecular_functionmetal ion binding
B0006783biological_processheme biosynthetic process
B0009055molecular_functionelectron transfer activity
B0016491molecular_functionoxidoreductase activity
B0020037molecular_functionheme binding
B0042597cellular_componentperiplasmic space
B0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues5
Detailsbinding site for residue BU3 A 501
ChainResidue
AASP214
AHOH611
AHOH630
BTRP199
BASP214

site_idAC2
Number of Residues15
Detailsbinding site for residue DHE A 502
ChainResidue
AARG164
AARG189
AASN190
AHIS323
APHE369
APHE370
AARG372
AHIS417
ATRP432
ATYR461
AHOH659
AARG36
AHIS147
AGLY149
ALYS151

site_idAC3
Number of Residues14
Detailsbinding site for residue HEC A 503
ChainResidue
AHIS12
ACYS13
ACYS16
AHIS17
APRO27
ALEU29
ALEU34
AILE46
AARG50
ATHR53
AGLN54
AMET55
APHE58
ATYR144

site_idAC4
Number of Residues16
Detailsbinding site for residue DHE B 501
ChainResidue
BARG36
BHIS147
BGLY148
BGLY149
BLYS151
BARG164
BARG189
BASN190
BTYR240
BHIS323
BPHE369
BPHE370
BARG372
BHIS417
BTYR461
BHOH601

site_idAC5
Number of Residues18
Detailsbinding site for Di-peptide HEC B 502 and CYS B 16
ChainResidue
BHIS12
BCYS13
BGLN14
BALA15
BHIS17
BGLY18
BGLY24
BSER25
BGLY26
BPRO27
BLEU29
BILE46
BARG50
BTHR53
BGLN54
BMET55
BPHE58
BTYR144

site_idAC6
Number of Residues15
Detailsbinding site for Di-peptide HEC B 502 and CYS B 13
ChainResidue
BTYR9
BHIS12
BGLN14
BALA15
BCYS16
BHIS17
BPRO27
BLEU29
BILE46
BARG50
BTHR53
BGLN54
BMET55
BPHE58
BTYR144

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsBINDING: covalent => ECO:0000255|PROSITE-ProRule:PRU00433, ECO:0000269|PubMed:31173777, ECO:0007744|PDB:6RTD, ECO:0007744|PDB:6RTE
ChainResidueDetails
ACYS13
ACYS16
BCYS13
BCYS16

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: axial binding residue => ECO:0000255|PROSITE-ProRule:PRU00433, ECO:0000269|PubMed:31173777, ECO:0007744|PDB:6RTD, ECO:0007744|PDB:6RTE
ChainResidueDetails
AHIS17
BHIS17

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:31173777, ECO:0007744|PDB:6RTD, ECO:0007744|PDB:6RTE
ChainResidueDetails
AARG50
BARG50

site_idSWS_FT_FI4
Number of Residues2
DetailsBINDING: axial binding residue => ECO:0000269|PubMed:31173777, ECO:0007744|PDB:6RTD, ECO:0007744|PDB:6RTE
ChainResidueDetails
AMET55
BMET55

site_idSWS_FT_FI5
Number of Residues2
DetailsBINDING: proximal binding residue => ECO:0000269|PubMed:31173777, ECO:0007744|PDB:6RTD
ChainResidueDetails
AHIS147
BHIS147

site_idSWS_FT_FI6
Number of Residues14
DetailsBINDING: BINDING => ECO:0000269|PubMed:31173777, ECO:0007744|PDB:6RTD
ChainResidueDetails
AGLY149
BARG164
BARG189
BASN190
BARG372
BHIS417
ALYS151
AARG164
AARG189
AASN190
AARG372
AHIS417
BGLY149
BLYS151

site_idSWS_FT_FI7
Number of Residues2
DetailsBINDING: distal binding residue => ECO:0000269|PubMed:31173777, ECO:0007744|PDB:6RTD
ChainResidueDetails
AHIS323
BHIS323

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PDB entries from 2024-07-31

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