eF-site ID 2izz-C PDB Code 2izz Chain C click to enlarge Title Crystal structure of human pyrroline-5-carboxylate reductase Classification OXIDOREDUCTASE Compound PYRROLINE-5-CARBOXYLATE REDUCTASE 1 Source Homo sapiens (Human) (P5CR1_HUMAN) Sequence C:  SMSVGFIGAGQLAFALAKGFTAAGVLAAHKIMASSPDMDL ATVSALRKMGVKLTPHNKETVQHSDVLFLAVKPHIIPFIL DEIGADIEDRHIVVSCAAGVTISSIEKKLSAFRPAPRVIR CMTNTPVVVREGATVYATGTHAQVEDGRLMEQLLSSVGFC TEVEEDLIDAVTGLSGSGPAYAFTALDALADGGVKMGLPR RLAVRLGAQALLGAAKMLLHSEQHPGQLKDNVSSPGGATI HALHVLESGGFRSLLINAVEASCIRTRELQSMADQE Description Functional site 1) chain C residue 6 type sequence I description BINDING SITE FOR RESIDUE NAD C 350 source : AC6 2) chain C residue 7 type sequence G description BINDING SITE FOR RESIDUE NAD C 350 source : AC6 3) chain C residue 8 type sequence A description BINDING SITE FOR RESIDUE NAD C 350 source : AC6 4) chain C residue 9 type sequence G description BINDING SITE FOR RESIDUE NAD C 350 source : AC6 5) chain C residue 10 type sequence Q description BINDING SITE FOR RESIDUE NAD C 350 source : AC6 6) chain C residue 11 type sequence L description BINDING SITE FOR RESIDUE NAD C 350 source : AC6 7) chain C residue 34 type sequence S description BINDING SITE FOR RESIDUE NAD C 350 source : AC6 8) chain C residue 35 type sequence P description BINDING SITE FOR RESIDUE NAD C 350 source : AC6 9) chain C residue 56 type sequence N description BINDING SITE FOR RESIDUE NAD C 350 source : AC6 10) chain C residue 69 type sequence A description BINDING SITE FOR RESIDUE NAD C 350 source : AC6 11) chain C residue 70 type sequence V description BINDING SITE FOR RESIDUE NAD C 350 source : AC6 12) chain C residue 71 type sequence K description BINDING SITE FOR RESIDUE NAD C 350 source : AC6 13) chain C residue 72 type sequence P description BINDING SITE FOR RESIDUE NAD C 350 source : AC6 14) chain C residue 78 type sequence I description BINDING SITE FOR RESIDUE NAD C 350 source : AC6 15) chain C residue 95 type sequence C description BINDING SITE FOR RESIDUE NAD C 350 source : AC6 16) chain C residue 96 type sequence A description BINDING SITE FOR RESIDUE NAD C 350 source : AC6 17) chain C residue 97 type sequence A description BINDING SITE FOR RESIDUE NAD C 350 source : AC6 18) chain C residue 122 type sequence T description BINDING SITE FOR RESIDUE NAD C 350 source : AC6 19) chain C residue 124 type sequence T description BINDING SITE FOR RESIDUE NAD C 350 source : AC6 20) chain C residue 231 type sequence V description BINDING SITE FOR RESIDUE EDO C1276 source : AC7 21) chain C residue 233 type sequence S description BINDING SITE FOR RESIDUE EDO C1276 source : AC7 22) chain C residue 238 type sequence T description BINDING SITE FOR RESIDUE EDO C1276 source : AC7 23) chain C residue 97 type sequence A description BINDING SITE FOR RESIDUE EDO C1277 source : AC8 24) chain C residue 171 type sequence T description BINDING SITE FOR RESIDUE EDO C1277 source : AC8 25) chain C residue 175 type sequence G description BINDING SITE FOR RESIDUE EDO C1277 source : AC8 26) chain C residue 230 type sequence N description BINDING SITE FOR RESIDUE NAD D 350 source : AC9 27) chain C residue 231 type sequence V description BINDING SITE FOR RESIDUE NAD D 350 source : AC9 28) chain C residue 233 type sequence S description BINDING SITE FOR RESIDUE NAD D 350 source : AC9 29) chain C residue 6 type BINDING sequence I description BINDING => ECO:0000269|Ref.18 source Swiss-Prot : SWS_FT_FI1 30) chain C residue 34 type BINDING sequence S description BINDING => ECO:0000269|Ref.18 source Swiss-Prot : SWS_FT_FI1 31) chain C residue 56 type BINDING sequence N description BINDING => ECO:0000269|Ref.18 source Swiss-Prot : SWS_FT_FI1 32) chain C residue 69 type BINDING sequence A description BINDING => ECO:0000269|Ref.18 source Swiss-Prot : SWS_FT_FI1 33) chain C residue 95 type BINDING sequence C description BINDING => ECO:0000269|Ref.18 source Swiss-Prot : SWS_FT_FI1 34) chain C residue 2 type MOD_RES sequence S description N-acetylserine => ECO:0000269|Ref.8, ECO:0000269|Ref.9, ECO:0007744|PubMed:19413330 source Swiss-Prot : SWS_FT_FI2

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