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5OFR

Structure of the antibacterial peptide ABC transporter McjD in a high energy outward occluded intermediate state

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0005524molecular_functionATP binding
A0005886cellular_componentplasma membrane
A0015031biological_processprotein transport
A0015421molecular_functionABC-type oligopeptide transporter activity
A0016020cellular_componentmembrane
A0016887molecular_functionATP hydrolysis activity
A0030153biological_processbacteriocin immunity
A0035672biological_processoligopeptide transmembrane transport
A0043213biological_processbacteriocin transport
A0055085biological_processtransmembrane transport
A0140359molecular_functionABC-type transporter activity
B0000166molecular_functionnucleotide binding
B0005524molecular_functionATP binding
B0005886cellular_componentplasma membrane
B0015031biological_processprotein transport
B0015421molecular_functionABC-type oligopeptide transporter activity
B0016020cellular_componentmembrane
B0016887molecular_functionATP hydrolysis activity
B0030153biological_processbacteriocin immunity
B0035672biological_processoligopeptide transmembrane transport
B0043213biological_processbacteriocin transport
B0055085biological_processtransmembrane transport
B0140359molecular_functionABC-type transporter activity
Functional Information from PDB Data
site_idAC1
Number of Residues16
Detailsbinding site for residue ADP A 601
ChainResidue
ATYR354
ATHR386
AMG602
AVO4603
BASN479
BASN480
BSER482
BGLN485
AILE360
APRO379
ASER380
AGLY381
ASER382
AGLY383
ALYS384
ASER385

site_idAC2
Number of Residues4
Detailsbinding site for residue MG A 602
ChainResidue
ASER385
AGLN426
AADP601
AVO4603

site_idAC3
Number of Residues13
Detailsbinding site for residue VO4 A 603
ChainResidue
ASER380
ALYS384
ASER385
AGLN426
AASP505
AGLU506
AHIS537
AADP601
AMG602
BSER482
BGLY483
BGLY484
BALA510

site_idAC4
Number of Residues18
Detailsbinding site for residue ADP B 601
ChainResidue
AVAL463
AASN464
AASN479
AASN480
ASER482
AGLN485
BTYR354
BILE360
BPRO379
BSER380
BGLY381
BSER382
BGLY383
BLYS384
BSER385
BTHR386
BMG602
BVO4603

site_idAC5
Number of Residues4
Detailsbinding site for residue MG B 602
ChainResidue
BSER385
BGLN426
BADP601
BVO4603

site_idAC6
Number of Residues12
Detailsbinding site for residue VO4 B 603
ChainResidue
ASER482
AGLY483
AGLY484
AALA510
BSER380
BLYS384
BSER385
BGLN426
BGLU506
BHIS537
BADP601
BMG602

Functional Information from PROSITE/UniProt
site_idPS00211
Number of Residues15
DetailsABC_TRANSPORTER_1 ABC transporters family signature. YSGGQKQRISLARLF
ChainResidueDetails
ATYR481-PHE495

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues240
DetailsTransmembrane: {"description":"Helical","evidences":[{"source":"PROSITE-ProRule","id":"PRU00441","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues574
DetailsDomain: {"description":"ABC transmembrane type-1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00441","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues466
DetailsDomain: {"description":"ABC transporter","evidences":[{"source":"PROSITE-ProRule","id":"PRU00434","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues14
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00434","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

247536

PDB entries from 2026-01-14

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