Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

4I8C

X-ray structure of NikA in complex with Ni-(L-His)2

Functional Information from GO Data
ChainGOidnamespacecontents
A0005515molecular_functionprotein binding
A0015675biological_processnickel cation transport
A0015833biological_processpeptide transport
A0016020cellular_componentmembrane
A0016151molecular_functionnickel cation binding
A0020037molecular_functionheme binding
A0030288cellular_componentouter membrane-bounded periplasmic space
A0042597cellular_componentperiplasmic space
A0043190cellular_componentATP-binding cassette (ABC) transporter complex
A0046914molecular_functiontransition metal ion binding
A0050919biological_processnegative chemotaxis
A0051540molecular_functionmetal cluster binding
A0055052cellular_componentATP-binding cassette (ABC) transporter complex, substrate-binding subunit-containing
A0055085biological_processtransmembrane transport
A0098716biological_processnickel cation import across plasma membrane
A1904680molecular_functionpeptide transmembrane transporter activity
B0005515molecular_functionprotein binding
B0015675biological_processnickel cation transport
B0015833biological_processpeptide transport
B0016020cellular_componentmembrane
B0016151molecular_functionnickel cation binding
B0020037molecular_functionheme binding
B0030288cellular_componentouter membrane-bounded periplasmic space
B0042597cellular_componentperiplasmic space
B0043190cellular_componentATP-binding cassette (ABC) transporter complex
B0046914molecular_functiontransition metal ion binding
B0050919biological_processnegative chemotaxis
B0051540molecular_functionmetal cluster binding
B0055052cellular_componentATP-binding cassette (ABC) transporter complex, substrate-binding subunit-containing
B0055085biological_processtransmembrane transport
B0098716biological_processnickel cation import across plasma membrane
B1904680molecular_functionpeptide transmembrane transporter activity
C0005515molecular_functionprotein binding
C0015675biological_processnickel cation transport
C0015833biological_processpeptide transport
C0016020cellular_componentmembrane
C0016151molecular_functionnickel cation binding
C0020037molecular_functionheme binding
C0030288cellular_componentouter membrane-bounded periplasmic space
C0042597cellular_componentperiplasmic space
C0043190cellular_componentATP-binding cassette (ABC) transporter complex
C0046914molecular_functiontransition metal ion binding
C0050919biological_processnegative chemotaxis
C0051540molecular_functionmetal cluster binding
C0055052cellular_componentATP-binding cassette (ABC) transporter complex, substrate-binding subunit-containing
C0055085biological_processtransmembrane transport
C0098716biological_processnickel cation import across plasma membrane
C1904680molecular_functionpeptide transmembrane transporter activity
Functional Information from PDB Data
site_idAC1
Number of Residues8
DetailsBINDING SITE FOR RESIDUE HIS A 601
ChainResidue
ATYR22
ATRP100
AARG137
ATRP398
AHIS416
AHIS602
ANI603
AHOH717

site_idAC2
Number of Residues9
DetailsBINDING SITE FOR RESIDUE HIS A 602
ChainResidue
AARG97
AARG137
ATYR382
AARG386
AHIS416
AHIS601
ANI603
AACT604
ATHR23

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE NI A 603
ChainResidue
AHIS416
AHIS601
AHIS602

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ACT A 604
ChainResidue
ATHR23
AGLU378
AHIS602
AHOH714

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE ACT A 605
ChainResidue
AGLN385
AHIS395
AHIS416
AHOH841
AHOH843
AHOH844

site_idAC6
Number of Residues3
DetailsBINDING SITE FOR RESIDUE ACT A 606
ChainResidue
ATYR127
AARG447
AHOH827

site_idAC7
Number of Residues2
DetailsBINDING SITE FOR RESIDUE ACT A 607
ChainResidue
ATHR203
AASP227

site_idAC8
Number of Residues2
DetailsBINDING SITE FOR RESIDUE ACT A 608
ChainResidue
APRO159
ALEU167

site_idAC9
Number of Residues1
DetailsBINDING SITE FOR RESIDUE ACT A 609
ChainResidue
AARG68

site_idBC1
Number of Residues2
DetailsBINDING SITE FOR RESIDUE ACT A 610
ChainResidue
AASN149
ALYS157

site_idBC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL A 611
ChainResidue
ATRP10
APRO11
AGLY219
AASN220
AGLY222
ALEU223

site_idBC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE GOL A 612
ChainResidue
AGLN361
ASER372
ALEU373

site_idBC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL A 613
ChainResidue
ALYS276
AGLU320
ATHR325
ALEU326
AARG333
BLYS276

site_idBC5
Number of Residues10
DetailsBINDING SITE FOR RESIDUE HIS B 601
ChainResidue
BTYR22
BTRP100
BARG137
BTRP398
BTYR402
BHIS416
BHIS602
BNI603
BHOH706
BHOH806

site_idBC6
Number of Residues10
DetailsBINDING SITE FOR RESIDUE HIS B 602
ChainResidue
BTYR22
BTHR23
BARG97
BARG137
BTYR382
BARG386
BHIS416
BHIS601
BNI603
BHOH825

site_idBC7
Number of Residues3
DetailsBINDING SITE FOR RESIDUE NI B 603
ChainResidue
BHIS416
BHIS601
BHIS602

site_idBC8
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL B 604
ChainResidue
BLEU293
BHIS459
BHOH728

site_idBC9
Number of Residues2
DetailsBINDING SITE FOR RESIDUE ACT B 605
ChainResidue
BSER57
BGLU58

site_idCC1
Number of Residues1
DetailsBINDING SITE FOR RESIDUE ACT B 606
ChainResidue
BTRP54

site_idCC2
Number of Residues2
DetailsBINDING SITE FOR RESIDUE ACT B 607
ChainResidue
BTHR441
BHIS442

site_idCC3
Number of Residues2
DetailsBINDING SITE FOR RESIDUE ACT B 608
ChainResidue
BASN149
BLYS157

site_idCC4
Number of Residues1
DetailsBINDING SITE FOR RESIDUE ACT B 609
ChainResidue
BGLU434

site_idCC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL B 610
ChainResidue
BASN220
BALA489
BTHR490
BHOH766
BHOH796

site_idCC6
Number of Residues1
DetailsBINDING SITE FOR RESIDUE GOL B 611
ChainResidue
BARG68

site_idCC7
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL B 612
ChainResidue
BLEU303
BGLY304
APHE229
ASER233
ALEU242
BASN302

site_idCC8
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SO4 B 613
ChainResidue
BTYR382
BGLN385
BPHE394
BHIS395
BARG396
BHIS416
BHOH755

site_idCC9
Number of Residues2
DetailsBINDING SITE FOR RESIDUE ACT B 614
ChainResidue
BARG341
CLYS433

site_idDC1
Number of Residues10
DetailsBINDING SITE FOR RESIDUE HIS C 601
ChainResidue
CTYR22
CMET27
CTRP100
CARG137
CTRP398
CTYR402
CHIS416
CHIS602
CNI603
CHOH709

site_idDC2
Number of Residues10
DetailsBINDING SITE FOR RESIDUE HIS C 602
ChainResidue
CTHR23
CARG97
CARG137
CTYR382
CARG386
CHIS416
CHIS601
CNI603
CHOH711
CHOH756

site_idDC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE NI C 603
ChainResidue
CHIS416
CHIS601
CHIS602

site_idDC4
Number of Residues2
DetailsBINDING SITE FOR RESIDUE ACT C 604
ChainResidue
CLYS275
CLYS276

site_idDC5
Number of Residues2
DetailsBINDING SITE FOR RESIDUE ACT C 605
ChainResidue
AARG95
CHIS442

site_idDC6
Number of Residues7
DetailsBINDING SITE FOR RESIDUE ACT C 606
ChainResidue
CTYR382
CGLN385
CPHE394
CHIS395
CARG396
CHIS416
CHOH755

site_idDC7
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL C 607
ChainResidue
CGLN361
CASP370
CVAL371
CSER372
CLEU373

site_idDC8
Number of Residues3
DetailsBINDING SITE FOR RESIDUE GOL C 608
ChainResidue
BASN261
CASN261
CHOH738

site_idDC9
Number of Residues2
DetailsBINDING SITE FOR RESIDUE SO4 C 609
ChainResidue
BLYS433
CARG341

Functional Information from PROSITE/UniProt
site_idPS01040
Number of Residues23
DetailsSBP_BACTERIAL_5 Bacterial extracellular solute-binding proteins, family 5 signature. AkswthseDgkTWtFtLRDDVKF
ChainResidueDetails
AALA51-PHE73

237992

PDB entries from 2025-06-25

PDB statisticsPDBj update infoContact PDBjnumon